2jh3

From Proteopedia

Revision as of 16:29, 5 November 2007

THE CRYSTAL STRUCTURE OF DR2241 FROM DEINOCOCCUS RADIODURANS AT 1.9 A RESOLUTION REVEALS A MULTI-DOMAIN PROTEIN WITH STRUCTURAL SIMILARITY TO CHELATASES BUT ALSO WITH TWO ADDITIONAL NOVEL DOMAINS

Overview

A unique family of proteins have been identified in the Deinococcus genus, with an N-terminal cobalamin (vitamin B(12)) chelatase domain denoted CbiX, and an additional unique C-terminal domain with unknown function. Here we, report the first crystal structure from this new family of proteins with, the structure of Deinococcus radiodurans protein DR2241. The structure, reveals a multi-domain protein where domains A (residues 1-132) has the, same fold as the small CbiX (CbiX(S)), domains A and B (residues 1-272), follow the chelatase super-family fold and the two additional unique, domains C and D have no structural homologues. Domain D harbours the, sequence motifs CxxC and CxxxC, in which DR2241 gives the first evidence, that these motifs bind a [4Fe-4S] iron-sulphur cluster. In solution there, are indications of multimeric forms, and in the crystallographic, asymmetric unit a tetramer is found where domains C and D are involved in, stabilising the tetrameric assembly.

About this Structure

2JH3 is a Single protein structure of sequence from Deinococcus radiodurans with SF4 as ligand. Structure known Active Site: AC1. Full crystallographic information is available from OCA.

Reference

The crystal structure of DR2241 from Deinococcus radiodurans at 1.9 A resolution reveals a multi-domain protein with structural similarity to chelatases but also with two additional novel domains., Leiros HK, McSweeney SM, J Struct Biol. 2007 Jul;159(1):92-102. Epub 2007 Mar 12. PMID:17448684

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