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STRUCTURE OF THE COBALT-DEPENDENT METHIONINE AMINOPEPTIDASE FROM ESCHERICHIA COLI: A NEW TYPE OF PROTEOLYTIC ENZYMESTRUCTURE OF THE COBALT-DEPENDENT METHIONINE AMINOPEPTIDASE FROM ESCHERICHIA COLI: A NEW TYPE OF PROTEOLYTIC ENZYME
Structural highlights
Function[AMPM_ECOLI] Removes the N-terminal methionine from nascent proteins. 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 X-ray structure of Escherichia coli methionine aminopeptidase (MAP) has been determined to 2.4-A resolution and refined to a crystallographic R-factor of 18.2%. The fold is novel and displays internal pseudo-2-fold symmetry which structurally relates the first and second halves of the polypeptide chain. The topology consists of a central antiparallel beta-sheet covered on one side by two pairs of alpha-helices and by a C-terminal loop. The other face of the beta-sheet, together with some irregular loops, forms the active site, which contains two cobalt ions 2.9 A apart. These metal ions are liganded by the side chains of Asp 97, Asp 108, Glu 204, Glu 235, and His 171 with approximate octahedral coordination. In terms of both the novel backbone fold and the constitution of the active site, MAP appears to represent a new class of proteolytic enzyme. Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzyme.,Roderick SL, Matthews BW Biochemistry. 1993 Apr 20;32(15):3907-12. PMID:8471602[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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