1qtr
From Proteopedia
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CRYSTAL STRUCTURE ANALYSIS OF THE PROLYL AMINOPEPTIDASE FROM SERRATIA MARCESCENS
Overview
Prolyl aminopeptidase from Serratia marcescens specifically catalyzes the, removal of N-terminal proline residues from peptides. We have solved its, three-dimensional structure at 2.3 A resolution by the multiple, isomorphous replacement method. The enzyme consists of two contiguous, domains. The larger domain shows the general topology of the alpha/beta, hydrolase fold, with a central eight-stranded beta-sheet and six helices., The smaller domain consists of six helices. The catalytic triad (Ser113, His296, and Asp268) is located near the large cavity at the interface, between the two domains. Cys271, which is sensitive to SH reagents, is, located near the catalytic residues, in spite of the fact that the enzyme, is a serine peptidase. The specific residues which make up the hydrophobic, pocket line the smaller domain, and the specificity of the exo-type enzyme, originates from this smaller domain, which blocks the N-terminal of P1, proline.
About this Structure
1QTR is a Single protein structure of sequence from Serratia marcescens. Active as Prolyl aminopeptidase, with EC number 3.4.11.5 Full crystallographic information is available from OCA.
Reference
Crystal structure of prolyl aminopeptidase from Serratia marcescens., Yoshimoto T, Kabashima T, Uchikawa K, Inoue T, Tanaka N, Nakamura KT, Tsuru M, Ito K, J Biochem (Tokyo). 1999 Sep;126(3):559-65. PMID:10467172
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