1ocm

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spinqualitylabelsall models 1ocm, resolution 1.9Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

THE CRYSTAL STRUCTURE OF MALONAMIDASE E2 COVALENTLY COMPLEXED WITH PYROPHOSPHATE FROM BRADYRHIZOBIUM JAPONICUM

Overview

A large group of hydrolytic enzymes, which contain a conserved stretch of, approximately 130 amino acids designated the amidase signature (AS), sequence, constitutes a super family that is distinct from any other known, hydrolase family. AS family enzymes are widespread in nature, ranging from, bacteria to humans, and exhibit a variety of biological functions. Here we, report the first structure of an AS family enzyme provided by the crystal, structure of malonamidase E2 from Bradyrhizobium japonicum. The structure, representing a new protein fold, reveals a previously unidentified, Ser-cisSer-Lys catalytic machinery that is absolutely conserved throughout, the family. This family of enzymes appears to be evolutionarily distinct, but has diverged to acquire a wide spectrum of individual ... [(full description)]

About this Structure

1OCM is a [Single protein] structure of sequence from [Bradyrhizobium japonicum] with POP as [ligand]. This structure superseeds the now removed PDB entry 1GRK. Structure known Active Site: PP1. Full crystallographic information is available from [OCA].

Reference

Structure of malonamidase E2 reveals a novel Ser-cisSer-Lys catalytic triad in a new serine hydrolase fold that is prevalent in nature., Shin S, Lee TH, Ha NC, Koo HM, Kim SY, Lee HS, Kim YS, Oh BH, EMBO J. 2002 Jun 3;21(11):2509-16. PMID:12032064

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