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1pvv

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Revision as of 07:37, 9 December 2020

Refined Structure of Pyrococcus furiosus Ornithine Carbamoyltransferase at 1.87 A

Structural highlights

1pvv is a 1 chain structure with sequence from Atcc 43587. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1a1s
Gene:	ARGF OR PF0594 (ATCC 43587)
Activity:	Ornithine carbamoyltransferase, with EC number 2.1.3.3
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[OTC_PYRFU] Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline, which is a substrate for argininosuccinate synthetase, the enzyme involved in the final step in arginine biosynthesis.^[1]

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

Using synchrotron radiation, X-ray data have been collected from Pyrococcus furiosus ornithine carbamoyltransferase (Pfu OTCase) to a maximal resolution of 1.87 A, allowing the refinement of a previous structure at 2.7 A [Villeret et al. (1998), Proc. Natl Acad. Sci. USA, 95, 2801-2806]. Thanks to the high resolution of this refined structure, two sulfate ions and 191 water molecules could be localized directly from the electron-density maps. The identification of these molecules allowed a more rigorous description of the active site and the identification of residues involved in binding carbamoyl phosphate. The improved quality of the model resulted in a better definition of several loops and the various interfaces. The dodecameric protein is composed of four catalytic trimers disposed in a tetrahedral manner. The extreme thermal stability of Pfu OTCase is mainly the result of the strengthening of the intersubunit interactions in a trimer and oligomerization of the trimers into a dodecamer. Interfaces between monomers in a catalytic trimer are characterized by an increase in ion-pair networks compared with mesophilic OTCases. However, the interfaces between catalytic trimers in the dodecameric oligomer are mainly hydrophobic and also involve aromatic-aromatic and cation-pi interactions.

Refined structure of Pyrococcus furiosus ornithine carbamoyltransferase at 1.87 A.,Massant J, Wouters J, Glansdorff N Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2140-9. Epub 2003, Nov 27. PMID:14646072^[2]

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

References

↑ Legrain C, Villeret V, Roovers M, Gigot D, Dideberg O, Pierard A, Glansdorff N. Biochemical characterisation of ornithine carbamoyltransferase from Pyrococcus furiosus. Eur J Biochem. 1997 Aug 1;247(3):1046-55. PMID:9288930
↑ Massant J, Wouters J, Glansdorff N. Refined structure of Pyrococcus furiosus ornithine carbamoyltransferase at 1.87 A. Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2140-9. Epub 2003, Nov 27. PMID:14646072

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==Refined Structure of Pyrococcus furiosus Ornithine Carbamoyltransferase at 1.87 A==
-<StructureSection load='1pvv' size='340' side='right' caption='[[1pvv]], [[Resolution|resolution]] 1.87&Aring;' scene=''>
+<StructureSection load='1pvv' size='340' side='right'caption='[[1pvv]], [[Resolution|resolution]] 1.87&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1pvv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43587 Atcc 43587]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PVV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PVV FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1pvv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43587 Atcc 43587]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PVV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1PVV FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a1s|1a1s]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1a1s|1a1s]]</div></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ARGF OR PF0594 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2261 ATCC 43587])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ornithine_carbamoyltransferase Ornithine carbamoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.3 2.1.3.3] </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=1pvv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pvv OCA], [http://pdbe.org/1pvv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pvv RCSB], [http://www.ebi.ac.uk/pdbsum/1pvv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pvv ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1pvv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pvv OCA], [http://pdbe.org/1pvv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pvv RCSB], [http://www.ebi.ac.uk/pdbsum/1pvv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pvv ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 31: / Line 31: @@
 </div>
 <div class="pdbe-citations 1pvv" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Ornithine carbamoyltransferase 3D structures|Ornithine carbamoyltransferase 3D structures]]
 == References ==
 <references/>
@@ Line 36: / Line 39: @@
 </StructureSection>
 [[Category: Atcc 43587]]
+[[Category: Large Structures]]
 [[Category: Ornithine carbamoyltransferase]]
 [[Category: Glansdorff, N]]

1pvv

From Proteopedia

Revision as of 07:37, 9 December 2020

Refined Structure of Pyrococcus furiosus Ornithine Carbamoyltransferase at 1.87 A

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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