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3vpb

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Revision as of 14:10, 5 August 2016

ArgX from Sulfolobus tokodaii complexed with LysW/Glu/ADP/Mg/Zn/Sulfate

Structural highlights

3vpb is a 6 chain structure with sequence from Sulto. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , ,
Related:	3vpc, 3vpd
Gene:	argE, STK_15050 (SULTO), lysW, STK_01925, STS023 (SULTO)
Activity:	Acetylornithine deacetylase, with EC number 3.5.1.16
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ARGX_SULTO] Catalyzes the ATP-dependent formation of a covalent bond between the amino group of glutamate and the gamma-carboxyl group of the C-terminal glutamate residue in LysW (By similarity). [LYSW_SULTO] Carrier protein that bears the covalently bound substrates for arginine and lysine biosynthesis; bound L-glutamate is sequentially converted to L-arginine, while bound alpha-aminoadipate (AAA) is sequentially converted to L-lysine.

Publication Abstract from PubMed

LysW has been identified as a carrier protein in the lysine biosynthetic pathway that is active through the conversion of alpha-aminoadipate (AAA) to lysine. In this study, we found that the hyperthermophilic archaeon, Sulfolobus acidocaldarius, not only biosynthesizes lysine through LysW-mediated protection of AAA but also uses LysW to protect the amino group of glutamate in arginine biosynthesis. In this archaeon, after LysW modification, AAA and glutamate are converted to lysine and ornithine, respectively, by a single set of enzymes with dual functions. The crystal structure of ArgX, the enzyme responsible for modification and protection of the amino moiety of glutamate with LysW, was determined in complex with LysW. Structural comparison and enzymatic characterization using Sulfolobus LysX, Sulfolobus ArgX and Thermus LysX identify the amino acid motif responsible for substrate discrimination between AAA and glutamate. Phylogenetic analysis reveals that gene duplication events at different stages of evolution led to ArgX and LysX.

Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus.,Ouchi T, Tomita T, Horie A, Yoshida A, Takahashi K, Nishida H, Lassak K, Taka H, Mineki R, Fujimura T, Kosono S, Nishiyama C, Masui R, Kuramitsu S, Albers SV, Kuzuyama T, Nishiyama M Nat Chem Biol. 2013 Apr;9(4):277-83. doi: 10.1038/nchembio.1200. Epub 2013 Feb, 24. PMID:23434852^[1]

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

References

↑ Ouchi T, Tomita T, Horie A, Yoshida A, Takahashi K, Nishida H, Lassak K, Taka H, Mineki R, Fujimura T, Kosono S, Nishiyama C, Masui R, Kuramitsu S, Albers SV, Kuzuyama T, Nishiyama M. Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus. Nat Chem Biol. 2013 Apr;9(4):277-83. doi: 10.1038/nchembio.1200. Epub 2013 Feb, 24. PMID:23434852 doi:10.1038/nchembio.1200

1 Structural highlights
2 Function
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/3vpb"

@@ Line 1: / Line 1: @@
 ==ArgX from Sulfolobus tokodaii complexed with LysW/Glu/ADP/Mg/Zn/Sulfate==
 <StructureSection load='3vpb' size='340' side='right' caption='[[3vpb]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3vpb]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulfolobus_tokodaii_str._7 Sulfolobus tokodaii str. 7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VPB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VPB FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3vpb]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulto Sulto]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VPB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VPB FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vpc|3vpc]], [[3vpd|3vpd]]</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">argE, STK_15050 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273063 Sulfolobus tokodaii str. 7]), lysW, STK_01925, STS023 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273063 Sulfolobus tokodaii str. 7])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">argE, STK_15050 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273063 SULTO]), lysW, STK_01925, STS023 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273063 SULTO])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetylornithine_deacetylase Acetylornithine deacetylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.16 3.5.1.16] </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=3vpb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vpb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vpb RCSB], [http://www.ebi.ac.uk/pdbsum/3vpb PDBsum]</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=3vpb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vpb OCA], [http://pdbe.org/3vpb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3vpb RCSB], [http://www.ebi.ac.uk/pdbsum/3vpb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3vpb ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 19: / Line 20: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3vpb" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
@@ Line 24: / Line 26: @@
 </StructureSection>
 [[Category: Acetylornithine deacetylase]]
-[[Category: Sulfolobus tokodaii str. 7]]
+[[Category: Sulto]]
 [[Category: Kuzuyama, T]]
 [[Category: Nishiyama, M]]

3vpb

From Proteopedia

Revision as of 14:10, 5 August 2016

ArgX from Sulfolobus tokodaii complexed with LysW/Glu/ADP/Mg/Zn/Sulfate

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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