2jh3
From Proteopedia
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==Overview== | ==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 . | + | 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== | ==About this Structure== | ||
| - | 2JH3 is a | + | 2JH3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans] with SF4 as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2JH3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:27:19 2007'' |
Revision as of 12:22, 5 November 2007
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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 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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