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2JH3

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

Summary for 2JH3
Entry DOI10.2210/pdb2jh3/pdb
DescriptorRIBOSOMAL PROTEIN S2-RELATED PROTEIN, IRON/SULFUR CLUSTER (3 entities in total)
Functional Keywordscbix, sad phasing, ribosomal protein, structural genomics, chelatase super-family fold, 4fe-4s iron-sulphur cluster
Biological sourceDEINOCOCCUS RADIODURANS
Total number of polymer chains4
Total formula weight205681.01
Authors
Leiros, H.-K.S.,Mcsweeney, S.M. (deposition date: 2007-02-20, release date: 2007-06-19, Last modification date: 2024-05-08)
Primary citationLeiros, H.-K.S.,Mcsweeney, S.M.
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
J.Struct.Biol., 159:92-, 2007
Cited by
PubMed Abstract: 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.
PubMed: 17448684
DOI: 10.1016/J.JSB.2007.02.009
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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数据于2025-12-24公开中

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