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4u5y

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Revision as of 16:31, 11 August 2016

Crystal Structure of the complex between the GNAT domain of S. lividans PAT and the acetyl-CoA synthetase C-terminal domain of S. enterica

Structural highlights

4u5y is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	4nxy
Activity:	Acetate--CoA ligase, with EC number 6.2.1.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[V1Q8H8_SALET] Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.[HAMAP-Rule:MF_01123] Enables the cell to use acetate during aerobic growth to generate energy via the TCA cycle, and biosynthetic compounds via the glyoxylate shunt. Acetylates CheY, the response regulator involved in flagellar movement and chemotaxis.[HAMAP-Rule:MF_01123]

Publication Abstract from PubMed

Reversible lysine acetylation by protein acetyltransferases is a conserved regulatory mechanism that controls diverse cellular pathways. Gcn5-related N-acetyltransferases (GNATs), named after their founding member, are found in all domains of life. GNATs are known for their role as histone acetyltransferases, but non-histone bacterial protein acetytransferases have been identified. Only structures of GNAT complexes with short histone peptide substrates are available in databases. Given the biological importance of this modification and the abundance of lysine in polypeptides, how specificity is attained for larger protein substrates is central to understanding acetyl-lysine regulated networks. Here we report the structure of a GNAT in complex with a globular protein substrate solved to 1.9 Angstrom. GNAT binds the protein substrate with extensive surface interactions distinct from those reported for GNAT-peptide complexes. Our data reveal determinants needed for the recognition of a protein substrate and provide insight into the specificity of GNATs.

Insights Into the Specificity of Lysine Acetyltransferases.,Tucker AC, Taylor KC, Rank KC, Rayment I, Escalante-Semerena JC J Biol Chem. 2014 Nov 7. pii: jbc.M114.613901. PMID:25381442^[1]

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

References

↑ Tucker AC, Taylor KC, Rank KC, Rayment I, Escalante-Semerena JC. Insights Into the Specificity of Lysine Acetyltransferases. J Biol Chem. 2014 Nov 7. pii: jbc.M114.613901. PMID:25381442 doi:http://dx.doi.org/10.1074/jbc.M114.613901

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4u5y"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of the complex between the GNAT domain of S. lividans PAT and the acetyl-CoA synthetase C-terminal domain of S. enterica==
 <StructureSection load='4u5y' size='340' side='right' caption='[[4u5y]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4nxy|4nxy]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetate--CoA_ligase Acetate--CoA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.1 6.2.1.1] </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=4u5y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u5y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4u5y RCSB], [http://www.ebi.ac.uk/pdbsum/4u5y 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=4u5y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u5y OCA], [http://pdbe.org/4u5y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4u5y RCSB], [http://www.ebi.ac.uk/pdbsum/4u5y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4u5y ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4u5y" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Acetyl-CoA synthetase|Acetyl-CoA synthetase]]
 == References ==
 <references/>

4u5y

From Proteopedia

Revision as of 16:31, 11 August 2016

Crystal Structure of the complex between the GNAT domain of S. lividans PAT and the acetyl-CoA synthetase C-terminal domain of S. enterica

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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