1smp
From Proteopedia
CRYSTAL STRUCTURE OF A COMPLEX BETWEEN SERRATIA MARCESCENS METALLO-PROTEASE AND AN INHIBITOR FROM ERWINIA CHRYSANTHEMI
Structural highlights
Function[PRZN_SERMA] Has insecticidal activity against the locust M.palpalis. When administered orally to locusts at a low dose it causes them to lie on their sides exhibiting sporadic limb movements and muscular twitching, followed by full recovery. When administered at higher doses the same symptoms are observed, followed by death. [INH_ERWCH] Inhibitor of the extracellular proteases A, B, and C of E.chrysanthemi and the S.marcescens 50 kDa extracellular protease. It forms a non-covalent bond with the proteases and may prevent autocatalytic cleavage of the proteases zymogen in the periplasm. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of the complex between the 50 kDa metallo-endoproteinase from Serratia marcescens (SMP), a member of the metzincin superfamily, and an inhibitor from Erwinia chrysanthemi (Inh) was solved by molecular replacement using the known structure of SMP, and refined at 2.30 A resolution to a crystallographic R-factor of 0.195. The E. chrysanthemi inhibitor folds into a compact eight-stranded antiparallel beta-barrel of simple up-down topology such as is found for members of the retinol binding protein family. It mainly interacts with the protease via its five N-terminal residues, which insert into the active site cleft, occupying the S' sites. The first N-terminal residue, SerI1, is partially cleaved off by the protease, while SerI2 makes a hydrogen bond with the catalytically active glutamic acid, Glu177, of the protease. Further interactions are made between one face of the inhibitor formed by the strands s3, s4 and s5 and the protease segment 218 to 228, which is located immediately after the characteristic "Met-turn" of the metzincins. Crystal structure of a complex between Serratia marcescens metallo-protease and an inhibitor from Erwinia chrysanthemi.,Baumann U, Bauer M, Letoffe S, Delepelaire P, Wandersman C J Mol Biol. 1995 May 5;248(3):653-61. PMID:7752231[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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