3gbo | pdb_00003gbo

Crystal structure of BmooMPalpha-I, a non-hemorrhagic metalloproteinase isolated from Bothrops moojeni snake venom

spinqualitylabelsall models 3gbo, resolution 1.77Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3gbo is a 1 chain structure with sequence from Bothrops moojeni. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [VM1BI_BOTMO] Snake venom zinc metalloproteinase that cleaves the alpha chain of fibrinogen (FGA) first followed by the beta chain (FGB) and shows no effect on the gamma chain. Cleaves only the beta chain of fibrin, leaving the gamma-dimer untouched. Shows proteolytic activity towards azocasein. Causes defibrinogenation when intraperitoneally administered on mice. 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 PubMed Hemostatically active snake venom metalloproteinases (SVMPs) perturb the blood coagulation cascade at specific points and due to their potential application as thrombolytic agents, the fibrin(ogen)olytic non-hemorrhagic SVMPs have been employed as biochemical tools in coagulation research and diagnosis. Structural studies complemented by the design of metalloproteinase inhibitors have been instrumental in understanding their stereo specificity and action mechanism. We present here, details of the crystal structure of BmooMPalpha-I, a 22.6 kDa non-hemorrhagic P-I class SVMP isolated from Bothrops moojeni venom, determined at 1.76 A resolution. In this structure, the catalytic zinc ion displays an unusual octahedral coordination formed by the three canonical histidines (His(142), His(146) and His(152)) and additionally, by three solvent molecules. Comparative sequence and structural studies indicate that the motif comprising amino acid segments 153-164 and 167-176 adjacent to the methionine-turn is a salient feature that differentiates both non and hemorrhagic P-I class SVMPs and could directly be involved in the development of the hemorrhagic activity. Structural studies of BmooMPalpha-I, a non-hemorrhagic metalloproteinase from Bothrops moojeni venom.,Akao PK, Tonoli CC, Navarro MS, Cintra AC, Neto JR, Arni RK, Murakami MT Toxicon. 2010 Feb-Mar;55(2-3):361-8. Epub 2009 Aug 23. PMID:19706302 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA