1vcn

From Proteopedia

(Difference between revisions)

Revision as of 07:10, 4 April 2018

Crystal Structure of T.th. HB8 CTP synthetase complex with Sulfate anion

Structural highlights

1vcn is a 1 chain structure with sequence from "flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1vcm, 1vco
Gene:	HB8 ("Flavobacterium thermophilum" Yoshida and Oshima 1971)
Activity:	CTP synthase (glutamine hydrolyzing), with EC number 6.3.4.2
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

[PYRG_THET8] Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen (By similarity).

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

CTP synthetase (CTPs) catalyzes the last step in CTP biosynthesis, in which ammonia generated at the glutaminase domain reacts with the ATP-phosphorylated UTP at the synthetase domain to give CTP. Glutamine hydrolysis is active in the presence of ATP and UTP and is stimulated by the addition of GTP. We report the crystal structures of Thermus thermophilus HB8 CTPs alone, CTPs with 3SO4(2-), and CTPs with glutamine. The enzyme is folded into a homotetramer with a cross-shaped structure. Based on the binding mode of sulfate anions to the synthetase site, ATP and UTP are computer modeled into CTPs with a geometry favorable for the reaction. Glutamine bound to the glutaminase domain is situated next to the triad of Glu-His-Cys as a catalyst and a water molecule. Structural information provides an insight into the conformational changes associated with the binding of ATP and UTP and the formation of the GTP binding site.

Crystal structures of CTP synthetase reveal ATP, UTP, and glutamine binding sites.,Goto M, Omi R, Nakagawa N, Miyahara I, Hirotsu K Structure. 2004 Aug;12(8):1413-23. PMID:15296735^[1]

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

References

↑ Goto M, Omi R, Nakagawa N, Miyahara I, Hirotsu K. Crystal structures of CTP synthetase reveal ATP, UTP, and glutamine binding sites. Structure. 2004 Aug;12(8):1413-23. PMID:15296735 doi:http://dx.doi.org/10.1016/j.str.2004.05.013

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==Crystal Structure of T.th. HB8 CTP synthetase complex with Sulfate anion==
 <StructureSection load='1vcn' size='340' side='right' caption='[[1vcn]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HB8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 "Flavobacterium thermophilum" Yoshida and Oshima 1971])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/CTP_synthase_(glutamine_hydrolyzing) CTP synthase (glutamine hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.2 6.3.4.2] </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=1vcn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vcn OCA], [http://pdbe.org/1vcn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1vcn RCSB], [http://www.ebi.ac.uk/pdbsum/1vcn PDBsum], [http://www.topsan.org/Proteins/RSGI/1vcn 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=1vcn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vcn OCA], [http://pdbe.org/1vcn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1vcn RCSB], [http://www.ebi.ac.uk/pdbsum/1vcn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1vcn ProSAT], [http://www.topsan.org/Proteins/RSGI/1vcn TOPSAN]</span></td></tr>
 </table>
 == Function ==
@@ Line 15: / Line 16: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vc/1vcn_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vc/1vcn_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=1vcn ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">

1vcn

From Proteopedia

Revision as of 07:10, 4 April 2018

Crystal Structure of T.th. HB8 CTP synthetase complex with Sulfate anion

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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