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PDBsum entry 1m93
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Viral protein
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PDB id
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1m93
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Viral protein
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Title:
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1.65 a structure of cleaved viral serpin crma
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Structure:
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Serine proteinase inhibitor 2. Chain: a. Fragment: residues 1-55. Synonym: cytokine response modifier protein a, serpin 2, serp-2, ice inhibitor, hemorrhage-inducing 38 kda protein. Engineered: yes. Serine proteinase inhibitor 2. Chain: b. Fragment: residues 56-300.
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Source:
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Cowpox virus. Organism_taxid: 10243. Gene: crma. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Biol. unit:
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Trimer (from
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Resolution:
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1.65Å
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R-factor:
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0.188
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R-free:
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0.245
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Authors:
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M.Simonovic,P.G.W.Gettins,K.Volz
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Key ref:
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M.Simonovic
et al.
(2000).
Crystal structure of viral serpin crmA provides insights into its mechanism of cysteine proteinase inhibition.
Protein Sci,
9,
1423-1427.
PubMed id:
DOI:
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Date:
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26-Jul-02
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Release date:
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05-Aug-03
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PROCHECK
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Headers
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References
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P07385
(SPI2_CWPXB) -
Serine proteinase inhibitor 2 from Cowpox virus (strain Brighton Red)
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Seq:
Struc:
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341 a.a.
46 a.a.
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Enzyme class:
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Chains A, B, C:
E.C.?
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DOI no:
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Protein Sci
9:1423-1427
(2000)
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PubMed id:
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Crystal structure of viral serpin crmA provides insights into its mechanism of cysteine proteinase inhibition.
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M.Simonovic,
Gettins PGW,
K.Volz.
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ABSTRACT
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CrmA is an unusual viral serpin that inhibits both cysteine and serine
proteinases involved in the regulation of host inflammatory and apoptosis
processes. It differs from other members of the serpin superfamily by having a
reactive center loop that is one residue shorter, and by its apparent inability
to form SDS-stable covalent complexes with cysteine proteinases. To obtain
insight into the inhibitory mechanism of crmA, we determined the crystal
structure of reactive center loop-cleaved crmA to 2.9 A resolution. The
structure, which is the first of a viral serpin, suggests that crmA can inhibit
cysteine proteinases by a mechanism analogous to that used by other serpins
against serine proteinases. However, one striking difference from other serpins,
which may be significant for in vivo function, is an additional highly charged
antiparallel strand for b sheet A, whose sequence and length are unique to crmA.
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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.Van Vliet,
M.R.Mohamed,
L.Zhang,
N.Y.Villa,
S.J.Werden,
J.Liu,
and
G.McFadden
(2009).
Poxvirus proteomics and virus-host protein interactions.
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Microbiol Mol Biol Rev,
73,
730-749.
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S.M.Best
(2008).
Viral subversion of apoptotic enzymes: escape from death row.
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Annu Rev Microbiol,
62,
171-192.
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T.H.Roberts,
and
J.Hejgaard
(2008).
Serpins in plants and green algae.
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Funct Integr Genomics,
8,
1.
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J.T.Christeller
(2005).
Evolutionary mechanisms acting on proteinase inhibitor variability.
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FEBS J,
272,
5710-5722.
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L.D.Tesch,
M.P.Raghavendra,
T.Bedsted-Faarvang,
P.G.Gettins,
and
S.T.Olson
(2005).
Specificity and reactive loop length requirements for crmA inhibition of serine proteases.
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Protein Sci,
14,
533-542.
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B.T.Seet,
J.B.Johnston,
C.R.Brunetti,
J.W.Barrett,
H.Everett,
C.Cameron,
J.Sypula,
S.H.Nazarian,
A.Lucas,
and
G.McFadden
(2003).
Poxviruses and immune evasion.
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Annu Rev Immunol,
21,
377-423.
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H.Everett,
and
G.McFadden
(2002).
Poxviruses and apoptosis: a time to die.
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Curr Opin Microbiol,
5,
395-402.
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H.R.Stennicke,
C.A.Ryan,
and
G.S.Salvesen
(2002).
Reprieval from execution: the molecular basis of caspase inhibition.
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Trends Biochem Sci,
27,
94.
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J.A.Irving,
R.N.Pike,
W.Dai,
D.Brömme,
D.M.Worrall,
G.A.Silverman,
T.H.Coetzer,
C.Dennison,
S.P.Bottomley,
and
J.C.Whisstock
(2002).
Evidence that serpin architecture intrinsically supports papain-like cysteine protease inhibition: engineering alpha(1)-antitrypsin to inhibit cathepsin proteases.
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Biochemistry,
41,
4998-5004.
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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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Links
