2jh3

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2jh3, resolution 1.90Å

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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 as ligand. Known structural/functional Site: . 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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