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PDBsum entry 2qhs
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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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Structural basis of octanoic acid recognition by lipoate-protein ligase b
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Structure:
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Lipoyltransferase. Chain: a. Synonym: lipb, lipoyl-[acyl-carrier-protein]-protein- n- lipoyltransferase, lipoate-protein ligase b. Engineered: yes
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Source:
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Thermus thermophilus. Organism_taxid: 300852. Strain: hb8. Gene: ttc 1746. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.50Å
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R-factor:
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0.187
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R-free:
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0.208
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Authors:
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D.J.Kim,S.J.Lee,H.S.Kim,K.H.Kim,H.H.Lee,H.J.Yoon,S.W.Suh
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Key ref:
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d.o. .J.Kim
et al.
(2008).
Structural basis of octanoic acid recognition by lipoate-protein ligase B.
Proteins,
70,
1620-1625.
PubMed id:
DOI:
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Date:
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02-Jul-07
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Release date:
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26-Feb-08
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PROCHECK
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Headers
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References
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Q5SLQ3
(LIPB_THET8) -
Octanoyltransferase from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
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Seq: Struc:
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217 a.a.
210 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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Enzyme class:
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E.C.2.3.1.181
- lipoyl(octanoyl) transferase.
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Reaction:
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octanoyl-[ACP] + L-lysyl-[protein] = N6-octanoyl-L-lysyl-[protein] + holo-[ACP] + H+
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octanoyl-[ACP]
Bound ligand (Het Group name = )
matches with 75.00% similarity
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+
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L-lysyl-[protein]
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=
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N(6)-octanoyl-L-lysyl-[protein]
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+
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holo-[ACP]
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Proteins
70:1620-1625
(2008)
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PubMed id:
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Structural basis of octanoic acid recognition by lipoate-protein ligase B.
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d.o. .J.Kim,
S.J.Lee,
H.S.Kim,
K.H.Kim,
H.H.Lee,
H.J.Yoon,
S.W.Suh.
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ABSTRACT
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Selected figure(s)
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Figure 1.
Figure 1. Overall fold and topology diagram of Tth LipB. (A)
F[o] - F[c] electron density maps of the bound ligands contoured
at 1.8 .
Atoms of the ligands are also labeled. All the figures are drawn
with PyMOL (DeLano, 2002, The PyMOL Molecular Graphics System,
http://www.pymol.org/). (B) Ribbon diagram. Secondary structure
elements were assigned by PROMOTIF.[19] -Helices,
-strands,
and loops are colored in cyan, yellow, and pink, respectively.
Octanoic acid bound near the center of LipB is shown in sticks.
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Figure 2.
Figure 2. Octanoic acid binding to Tth LipB. (A) Stereo view of
the active site around the bound octanoic acid. Black dotted
lines denote hydrogen bonds (B) Ribbon diagram of the crystal
structure of Mtu LipB[11] and the homology model of E. coli
LipB. -Helices,
-strands,
and loops are colored in cyan, yellow, and pink, respectively.
Decanoic acid and octanoic acid bound to each of the two
proteins are shown in sticks.
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The above figures are
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2008,
70,
1620-1625)
copyright 2008.
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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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Q.H.Christensen,
and
J.E.Cronan
(2009).
The Thermoplasma acidophilum LplA-LplB Complex Defines a New Class of Bipartite Lipoate-protein Ligases.
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J Biol Chem,
284,
21317-21326.
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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.
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