1su2

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(Difference between revisions)

Revision as of 07:37, 14 March 2018

CRYSTAL STRUCTURE OF THE NUDIX HYDROLASE DR1025 IN COMPLEX WITH ATP

Structural highlights

1su2 is a 2 chain structure with sequence from "micrococcus_radiodurans"_raj_et_al._1960 "micrococcus radiodurans" raj et al. 1960. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Gene:	DR1025 ("Micrococcus radiodurans" Raj et al. 1960)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ranatunga W, Hill EE, Mooster JL, Holbrook EL, Schulze-Gahmen U, Xu W, Bessman MJ, Brenner SE, Holbrook SR. Structural studies of the Nudix hydrolase DR1025 from Deinococcus radiodurans and its ligand complexes. J Mol Biol. 2004 May 21;339(1):103-16. PMID:15123424 doi:http://dx.doi.org/10.1016/j.jmb.2004.01.065

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1su2"

@@ Line 1: / Line 1: @@
 ==CRYSTAL STRUCTURE OF THE NUDIX HYDROLASE DR1025 IN COMPLEX WITH ATP==
 <StructureSection load='1su2' size='340' side='right' caption='[[1su2]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</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=1su2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1su2 OCA], [http://pdbe.org/1su2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1su2 RCSB], [http://www.ebi.ac.uk/pdbsum/1su2 PDBsum], [http://www.topsan.org/Proteins/BSGC/1su2 TOPSAN]</span></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=1su2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1su2 OCA], [http://pdbe.org/1su2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1su2 RCSB], [http://www.ebi.ac.uk/pdbsum/1su2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1su2 ProSAT], [http://www.topsan.org/Proteins/BSGC/1su2 TOPSAN]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 11: / Line 12: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/su/1su2_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/su/1su2_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1su2 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">

1su2

From Proteopedia

Revision as of 07:37, 14 March 2018

CRYSTAL STRUCTURE OF THE NUDIX HYDROLASE DR1025 IN COMPLEX WITH ATP

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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