1ibq | pdb_00001ibq

ASPERGILLOPEPSIN FROM ASPERGILLUS PHOENICIS

spinqualitylabelsall models 1ibq, resolution 2.14Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ibq is a 2 chain structure with sequence from Aspergillus phoenicis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MAN, ZN Related: 3app, 4ape, 2apr, 1psn, 1eag, 1mpp Activity: Aspergillopepsin I, with EC number 3.4.23.18 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PEPA_ASPPH] Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. Can catalyze hydrolysis of the major structural proteins of basement membrane, elastin, collagen, and laminin (By similarity). 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 The crystal structure of aspergillopepsin I (AP) from Aspergillus phoenicis has been determined at 2.18 A resolution and refined to R and R(free) factors of 21.5 and 26.0%, respectively. AP has the typical two beta-barrel domain structure of aspartic proteinases. The structures of the two independent molecules are partly different, exemplifying the flexible nature of the aspartic proteinase structure. Notably, the 'flap' in one molecule is closer, with a largest separation of 4.0 A, to the active site than in the other molecule. AP is most structurally homologous to penicillopepsin (PP) and then to endothiapepsin (EP), which share sequence identities of 68 and 56%, respectively. However, AP is similar to EP but differs from PP in the combined S1'-S2 subsite that is delineated by a flexible psi-loop in the C-terminal domain. The S1' and S2 subsites are well defined and small in AP, while there is no definite border between S1' and S2 and the open space for the S2 subsite is larger in PP. Comparison of the structures indicates that the two amino-acid residues equivalent to Leu295 and Leu297 of AP are the major determining factors in shaping the S1'-S2 subsite in the fungal aspartic proteinases. Structure of aspergillopepsin I from Aspergillus phoenicis: variations of the S1'-S2 subsite in aspartic proteinases.,Cho SW, Kim N, Choi MU, Shin W Acta Crystallogr D Biol Crystallogr. 2001 Jul;57(Pt 7):948-56. Epub 2001, Jun 21. PMID:11418762 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pepsin

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