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PDBsum entry 2uv5
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* Residue conservation analysis
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PDB id:
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Transferase
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Title:
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Crystal structure of a cbs domain pair from the regulatory gamma1 subunit of human ampk in complex with amp
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Structure:
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5'-amp-activated protein kinase subunit gamma-1. Chain: a. Fragment: cbs 3 and 4 fragment, residues 182-325. Synonym: ampk gamma-1 chain, ampkg, ampk gamma1 chain cbs domains 3 and 4. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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1.69Å
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R-factor:
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0.171
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R-free:
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0.227
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Authors:
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P.Day,A.Sharff,L.Parra,A.Cleasby,M.Williams,S.Horer,H.Nar,N.Redemann, I.Tickle,J.Yon
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Key ref:
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P.Day
et al.
(2007).
Structure of a CBS-domain pair from the regulatory gamma1 subunit of human AMPK in complex with AMP and ZMP.
Acta Crystallogr D Biol Crystallogr,
63,
587-596.
PubMed id:
DOI:
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Date:
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09-Mar-07
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Release date:
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08-May-07
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PROCHECK
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Headers
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References
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P54619
(AAKG1_HUMAN) -
5'-AMP-activated protein kinase subunit gamma-1 from Homo sapiens
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Seq: Struc:
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331 a.a.
144 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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DOI no:
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Acta Crystallogr D Biol Crystallogr
63:587-596
(2007)
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PubMed id:
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Structure of a CBS-domain pair from the regulatory gamma1 subunit of human AMPK in complex with AMP and ZMP.
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P.Day,
A.Sharff,
L.Parra,
A.Cleasby,
M.Williams,
S.Hörer,
H.Nar,
N.Redemann,
I.Tickle,
J.Yon.
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ABSTRACT
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AMP-activated kinase (AMPK) is central to sensing energy status in eukaryotic
cells via binding of AMP and ATP to CBS (cystathionine beta-synthase) domains in
the regulatory gamma subunit. The structure of a CBS-domain pair from human AMPK
gamma1 in complex with the physiological activator AMP and the pharmacological
activator ZMP (AICAR) is presented.
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Selected figure(s)
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Figure 1.
Figure 1 The structure of AMPK 1
CBS domains 3 and 4. (a) Cartoon representation of the structure
with bound AMP and |F[o]| - |F[c]| density for the ligand. (b)
The crystallographic dimer.
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Figure 5.
Figure 5 Superposition of AMPK CBS3+4
(green) and IMPDH CBS domains (PDB code 1zfj , red). AMP is from
the AMPK structure. Highlighted residues are 1, His298 (Ser123);
2, Ser316 (Arg143); 3, Ser314 (Thr141); 4, Asp317 (Asp144); 5,
Thr200 (Thr160); 6, Ile312 (Ile139); 7, Ile204 (Leu164); 8,
Val225 (Ile185); 9, Ser226 (Glu186); 10, Ala227 (Lys187); 11,
Arg299 (Gly124). Residues in parentheses are from IMPDH.
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2007,
63,
587-596)
copyright 2007.
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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J.Jämsen,
H.Tuominen,
A.A.Baykov,
and
R.Lahti
(2011).
Mutational analysis of residues in the regulatory CBS domains of Moorella thermoacetica pyrophosphatase corresponding to disease-related residues of human proteins.
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Biochem J,
433,
497-504.
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L.A.Martínez-Cruz,
J.A.Encinar,
P.Sevilla,
I.Oyenarte,
I.Gómez-García,
D.Aguado-Llera,
F.García-Blanco,
J.Gómez,
and
J.L.Neira
(2011).
Nucleotide-induced conformational transitions in the CBS domain protein MJ0729 of Methanocaldococcus jannaschii.
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Protein Eng Des Sel,
24,
161-169.
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S.A.Hawley,
F.A.Ross,
C.Chevtzoff,
K.A.Green,
A.Evans,
S.Fogarty,
M.C.Towler,
L.J.Brown,
O.A.Ogunbayo,
A.M.Evans,
and
D.G.Hardie
(2010).
Use of cells expressing gamma subunit variants to identify diverse mechanisms of AMPK activation.
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Cell Metab,
11,
554-565.
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B.C.Jeong,
K.S.Yoo,
K.W.Jung,
J.S.Shin,
and
H.K.Song
(2008).
Purification, crystallization and preliminary X-ray diffraction analysis of a cystathionine beta-synthase domain-containing protein, CDCP2, from Arabidopsis thaliana.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
64,
825-827.
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G.Q.Martinez,
and
M.Maduke
(2008).
A cytoplasmic domain mutation in ClC-Kb affects long-distance communication across the membrane.
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PLoS ONE,
3,
e2746.
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M.Lucas,
D.Kortazar,
E.Astigarraga,
J.A.Fernández,
J.M.Mato,
M.L.Martínez-Chantar,
and
L.A.Martínez-Cruz
(2008).
Purification, crystallization and preliminary X-ray diffraction analysis of the CBS-domain pair from the Methanococcus jannaschii protein MJ0100.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
64,
936-941.
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M.Pimkin,
and
G.D.Markham
(2008).
The CBS subdomain of inosine 5'-monophosphate dehydrogenase regulates purine nucleotide turnover.
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Mol Microbiol,
68,
342-359.
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M.Proudfoot,
S.A.Sanders,
A.Singer,
R.Zhang,
G.Brown,
A.Binkowski,
L.Xu,
J.A.Lukin,
A.G.Murzin,
A.Joachimiak,
C.H.Arrowsmith,
A.M.Edwards,
A.V.Savchenko,
and
A.F.Yakunin
(2008).
Biochemical and structural characterization of a novel family of cystathionine beta-synthase domain proteins fused to a Zn ribbon-like domain.
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J Mol Biol,
375,
301-315.
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PDB codes:
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P.Fernández-Millán,
D.Kortazar,
M.Lucas,
M.L.Martínez-Chantar,
E.Astigarraga,
J.A.Fernández,
O.Sabas,
A.Albert,
J.M.Mato,
and
L.A.Martínez-Cruz
(2008).
Crystallization and preliminary crystallographic analysis of merohedrally twinned crystals of MJ0729, a CBS-domain protein from Methanococcus jannaschii.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
64,
605-609.
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S.E.Mortimer,
D.Xu,
D.McGrew,
N.Hamaguchi,
H.C.Lim,
S.J.Bowne,
S.P.Daiger,
and
L.Hedstrom
(2008).
IMP Dehydrogenase Type 1 Associates with Polyribosomes Translating Rhodopsin mRNA.
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J Biol Chem,
283,
36354-36360.
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U.Riek,
R.Scholz,
P.Konarev,
A.Rufer,
M.Suter,
A.Nazabal,
P.Ringler,
M.Chami,
S.A.Müller,
D.Neumann,
M.Forstner,
M.Hennig,
R.Zenobi,
A.Engel,
D.Svergun,
U.Schlattner,
and
T.Wallimann
(2008).
Structural properties of AMP-activated protein kinase: dimerization, molecular shape, and changes upon ligand binding.
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J Biol Chem,
283,
18331-18343.
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D.G.Hardie
(2007).
AMP-activated/SNF1 protein kinases: conserved guardians of cellular energy.
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Nat Rev Mol Cell Biol,
8,
774-785.
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G.A.Amodeo,
M.J.Rudolph,
and
L.Tong
(2007).
Crystal structure of the heterotrimer core of Saccharomyces cerevisiae AMPK homologue SNF1.
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Nature,
449,
492-495.
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PDB code:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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