1M93: 1.65 A Structure Of Cleaved Viral Serpin Crma

Citation:
Abstract
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.
PDB ID: 1M93Download
MMDB ID: 24141
PDB Deposition Date: 2002/7/26
Updated in MMDB: 2007/10
Experimental Method:
x-ray diffraction
Resolution: 1.65  Å
Source Organism:
Similar Structures:
Biological Unit for 1M93: trimeric; determined by author and by software (PISA)
Molecular Components in 1M93
Label Count Molecule
Proteins (3 molecules)
1
Serine Proteinase Inhibitor 2(Gene symbol: CrmA)
Molecule annotation
1
Serine Proteinase Inhibitor 2(Gene symbol: CrmA)
Molecule annotation
1
Serine Proteinase Inhibitor 2(Gene symbol: CrmA)
Molecule annotation
Chemical (1 molecule)
1
1
* Click molecule labels to explore molecular sequence information.

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