1sz3

<StructureSection load='1sz3' size='340' side='right' caption='[[1sz3]], [[Resolution|resolution]] 1.60&Aring;' scene=''>

<table><tr><td colspan='2'>[[1sz3]] is a 2 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=1SZ3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SZ3 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1sz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sz3 OCA], [http://pdbe.org/1sz3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sz3 RCSB], [http://www.ebi.ac.uk/pdbsum/1sz3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1sz3 ProSAT], [http://www.topsan.org/Proteins/BSGC/1sz3 TOPSAN]</span></td></tr>

<div style="background-color:#fffaf0;">

== 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 1sz3" 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]]