2p20: Difference between revisions

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[[Image:2p20.png|left|200px]]


{{STRUCTURE_2p20|  PDB=2p20  |  SCENE=  }}
==Acetyl-CoA Synthetase, R584A mutation==
 
<StructureSection load='2p20' size='340' side='right'caption='[[2p20]], [[Resolution|resolution]] 2.22&Aring;' scene=''>
===Acetyl-CoA Synthetase, R584A mutation===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[2p20]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P20 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P20 FirstGlance]. <br>
{{ABSTRACT_PUBMED_17497934}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.22&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PRX:ADENOSINE-5-MONOPHOSPHATE-PROPYL+ESTER'>PRX</scene></td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2p20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p20 OCA], [https://pdbe.org/2p20 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p20 RCSB], [https://www.ebi.ac.uk/pdbsum/2p20 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p20 ProSAT]</span></td></tr>
[[2p20]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_typhimurium Salmonella enterica subsp. enterica serovar typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P20 OCA].  
</table>
== Function ==
[https://www.uniprot.org/uniprot/ACSA_SALTY ACSA_SALTY] 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.<ref>PMID:17497934</ref>  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 (By similarity).<ref>PMID:17497934</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p2/2p20_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/main_output.php?pdb_ID=2p20 ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Acetyl-CoA synthetase|Acetyl-CoA synthetase]]
*[[Acetyl-CoA synthetase 3D structures|Acetyl-CoA synthetase 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:017497934</ref><references group="xtra"/>
__TOC__
[[Category: Acetate--CoA ligase]]
</StructureSection>
[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]
[[Category: Large Structures]]
[[Category: Gulick, A M.]]
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
[[Category: Reger, A S.]]
[[Category: Gulick AM]]
[[Category: Acyl-coa ligase]]
[[Category: Reger AS]]
[[Category: Adenylate-forming enzyme]]
[[Category: Domain alternation]]
[[Category: Ligase]]

Latest revision as of 16:53, 13 March 2024

Acetyl-CoA Synthetase, R584A mutationAcetyl-CoA Synthetase, R584A mutation

Structural highlights

2p20 is a 2 chain structure with sequence from Salmonella enterica subsp. enterica serovar Typhimurium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.22Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ACSA_SALTY 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.[1] 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 (By similarity).[2]

Evolutionary Conservation

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

See Also

References

  1. Reger AS, Carney JM, Gulick AM. Biochemical and crystallographic analysis of substrate binding and conformational changes in acetyl-CoA synthetase. Biochemistry. 2007 Jun 5;46(22):6536-46. Epub 2007 May 12. PMID:17497934 doi:http://dx.doi.org/10.1021/bi6026506
  2. Reger AS, Carney JM, Gulick AM. Biochemical and crystallographic analysis of substrate binding and conformational changes in acetyl-CoA synthetase. Biochemistry. 2007 Jun 5;46(22):6536-46. Epub 2007 May 12. PMID:17497934 doi:http://dx.doi.org/10.1021/bi6026506

2p20, resolution 2.22Å

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