2p2m: Difference between revisions

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[[Image:2p2m.png|left|200px]]


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==Acetyl-CoA Synthetase, R194A mutation==
The line below this paragraph, containing "STRUCTURE_2p2m", creates the "Structure Box" on the page.
<StructureSection load='2p2m' size='340' side='right'caption='[[2p2m]], [[Resolution|resolution]] 2.11&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2p2m]] 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=2P2M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P2M FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.11&#8491;</td></tr>
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<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>
{{STRUCTURE_2p2m| PDB=2p2m |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2p2m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p2m OCA], [https://pdbe.org/2p2m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p2m RCSB], [https://www.ebi.ac.uk/pdbsum/2p2m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p2m ProSAT]</span></td></tr>
</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/p2/2p2m_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=2p2m ConSurf].
<div style="clear:both"></div>


===Acetyl-CoA Synthetase, R194A mutation===
==See Also==
 
*[[Acetyl-CoA synthetase 3D structures|Acetyl-CoA synthetase 3D structures]]
 
== References ==
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[[Category: Large Structures]]
{{ABSTRACT_PUBMED_17497934}}
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
 
[[Category: Gulick AM]]
==About this Structure==
[[Category: Reger AS]]
2P2M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P2M OCA].
 
==Reference==
Biochemical and crystallographic analysis of substrate binding and conformational changes in acetyl-CoA synthetase., Reger AS, Carney JM, Gulick AM, Biochemistry. 2007 Jun 5;46(22):6536-46. Epub 2007 May 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17497934 17497934]
[[Category: Acetate--CoA ligase]]
[[Category: Salmonella typhimurium]]
[[Category: Single protein]]
[[Category: Gulick, A M.]]
[[Category: Reger, A S.]]
[[Category: Acyl-coa ligase]]
[[Category: Adenylate-forming enzyme]]
[[Category: Domain alternation]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:07:04 2008''

Latest revision as of 12:07, 21 February 2024

Acetyl-CoA Synthetase, R194A mutationAcetyl-CoA Synthetase, R194A mutation

Structural highlights

2p2m 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 2.11Å
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

2p2m, resolution 2.11Å

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