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PDBsum entry 3m1i
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Protein transport
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PDB id
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3m1i
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Contents |
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200 a.a.
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131 a.a.
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1023 a.a.
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* Residue conservation analysis
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PDB id:
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Protein transport
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Title:
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Crystal structure of yeast crm1 (xpo1p) in complex with yeast ranbp1 (yrb1p) and yeast rangtp (gsp1pgtp)
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Structure:
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Gtp-binding nuclear protein gsp1/cnr1. Chain: a. Synonym: rangtp, gsp1pgtp, gtpase ran homolog, genetic suppressor of prp20-1, chromosome stability protein 17. Engineered: yes. Mutation: yes. Ran-specific gtpase-activating protein 1. Chain: b. Synonym: yrb1p, ran-binding protein 1, ranbp1, perinuclear array-
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Source:
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Saccharomyces cerevisiae. Yeast. Organism_taxid: 4932. Gene: gsp1. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: yrb1. Gene: xpo1.
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Resolution:
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2.00Å
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R-factor:
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0.178
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R-free:
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0.220
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Authors:
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M.Koyama,Y.Matsuura
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Key ref:
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M.Koyama
and
Y.Matsuura
(2010).
An allosteric mechanism to displace nuclear export cargo from CRM1 and RanGTP by RanBP1.
Embo J,
29,
2002-2013.
PubMed id:
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Date:
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05-Mar-10
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Release date:
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02-Jun-10
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PROCHECK
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Headers
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References
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P32835
(GSP1_YEAST) -
GTP-binding nuclear protein GSP1/CNR1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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219 a.a.
200 a.a.*
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Enzyme class:
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Chains A, B, C:
E.C.?
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Embo J
29:2002-2013
(2010)
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PubMed id:
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An allosteric mechanism to displace nuclear export cargo from CRM1 and RanGTP by RanBP1.
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M.Koyama,
Y.Matsuura.
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ABSTRACT
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The karyopherin CRM1 mediates nuclear export of proteins and ribonucleoproteins
bearing a leucine-rich nuclear export signal (NES). To elucidate the precise
mechanism by which NES-cargos are dissociated from CRM1 in the cytoplasm, which
is important for transport directionality, we determined a 2.0-A resolution
crystal structure of yeast CRM1:RanBP1:RanGTP complex, an intermediate in the
disassembly of the CRM1 nuclear export complex. The structure shows that on
association of Ran-binding domain (RanBD) of RanBP1 with CRM1:NES-cargo:RanGTP
complex, RanBD and the C-terminal acidic tail of Ran induce a large movement of
the intra-HEAT9 loop of CRM1. The loop moves to the CRM1 inner surface
immediately behind the NES-binding site and causes conformational rearrangements
in HEAT repeats 11 and 12 so that the hydrophobic NES-binding cleft on the CRM1
outer surface closes, squeezing out the NES-cargo. This allosteric mechanism
accelerates dissociation of NES by over two orders of magnitude. Structure-based
mutagenesis indicated that the HEAT9 loop also functions as an allosteric
autoinhibitor to stabilize CRM1 in a conformation that is unable to bind
NES-cargo in the absence of RanGTP.
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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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K.Langer,
C.Dian,
V.Rybin,
C.W.Müller,
and
C.Petosa
(2011).
Insights into the Function of the CRM1 Cofactor RanBP3 from the Structure of Its Ran-Binding Domain.
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PLoS One,
6,
e17011.
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PDB codes:
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S.J.Lee,
C.Jiko,
E.Yamashita,
and
T.Tsukihara
(2011).
Selective nuclear export mechanism of small RNAs.
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Curr Opin Struct Biol,
21,
101-108.
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T.Güttler,
T.Madl,
P.Neumann,
D.Deichsel,
L.Corsini,
T.Monecke,
R.Ficner,
M.Sattler,
and
D.Görlich
(2010).
NES consensus redefined by structures of PKI-type and Rev-type nuclear export signals bound to CRM1.
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Nat Struct Mol Biol,
17,
1367-1376.
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PDB codes:
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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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Links
