1soi

<StructureSection load='1soi' size='340' side='right' caption='[[1soi]], [[Resolution|resolution]] 1.80&Aring;' scene=''>

<table><tr><td colspan='2'>[[1soi]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_radiodurans"_raj_et_al._1960 "micrococcus radiodurans" raj et al. 1960]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SOI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SOI FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SM:SAMARIUM+(III)+ION'>SM</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DR1025 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1299 "Micrococcus radiodurans" Raj et al. 1960])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1soi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1soi OCA], [http://pdbe.org/1soi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1soi RCSB], [http://www.ebi.ac.uk/pdbsum/1soi PDBsum], [http://www.topsan.org/Proteins/BSGC/1soi TOPSAN]</span></td></tr>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/so/1soi_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

We have determined the crystal structure, at 1.4A, of the Nudix hydrolase DR1025 from the extremely radiation resistant bacterium Deinococcus radiodurans. The protein forms an intertwined homodimer by exchanging N-terminal segments between chains. We have identified additional conserved elements of the Nudix fold, including the metal-binding motif, a kinked beta-strand characterized by a proline two positions upstream of the Nudix consensus sequence, and participation of the N-terminal extension in the formation of the substrate-binding pocket. Crystal structures were also solved of DR1025 crystallized in the presence of magnesium and either a GTP analog or Ap(4)A (both at 1.6A resolution). In the Ap(4)A co-crystal, the electron density indicated that the product of asymmetric hydrolysis, ATP, was bound to the enzyme. The GTP analog bound structure showed that GTP was bound almost identically as ATP. Neither nucleoside triphosphate was further cleaved.

Structural studies of the Nudix hydrolase DR1025 from Deinococcus radiodurans and its ligand complexes.,Ranatunga W, Hill EE, Mooster JL, Holbrook EL, Schulze-Gahmen U, Xu W, Bessman MJ, Brenner SE, Holbrook SR J Mol Biol. 2004 May 21;339(1):103-16. PMID:15123424<ref>PMID:15123424</ref>

<div class="pdbe-citations 1soi" style="background-color:#fffaf0;"></div>

[[Category: Micrococcus radiodurans raj et al. 1960]]

[[Category: Structural genomic]]

[[Category: Bessman, M J]]

[[Category: Brenner, S E]]

[[Category: Hill, E E]]

[[Category: Holbrook, E L]]

[[Category: Holbrook, S R]]

[[Category: Mooster, J L]]

[[Category: Ranatunga, W]]

[[Category: Schulze-Gahmen, U]]

[[Category: Xu, W]]

[[Category: PSI, Protein structure initiative]]