1pg4: Difference between revisions

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{{Seed}}
[[Image:1pg4.png|left|200px]]


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==Acetyl CoA Synthetase, Salmonella enterica==
The line below this paragraph, containing "STRUCTURE_1pg4", creates the "Structure Box" on the page.
<StructureSection load='1pg4' size='340' side='right'caption='[[1pg4]], [[Resolution|resolution]] 1.75&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'>[[1pg4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica Salmonella enterica]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1nnm 1nnm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PG4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PG4 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]] 1.75&#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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PRX:ADENOSINE-5-MONOPHOSPHATE-PROPYL+ESTER'>PRX</scene></td></tr>
{{STRUCTURE_1pg4| PDB=1pg4 |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pg4 OCA], [https://pdbe.org/1pg4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pg4 RCSB], [https://www.ebi.ac.uk/pdbsum/1pg4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pg4 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/pg/1pg4_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=1pg4 ConSurf].
<div style="clear:both"></div>


===Acetyl CoA Synthetase, Salmonella enterica===
==See Also==
 
*[[Acetyl-CoA synthetase 3D structures|Acetyl-CoA synthetase 3D structures]]
 
== References ==
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(as it appears on PubMed at http://www.pubmed.gov), where 12627952 is the PubMed ID number.
</StructureSection>
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[[Category: Large Structures]]
{{ABSTRACT_PUBMED_12627952}}
 
==About this Structure==
1PG4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica Salmonella enterica]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1nnm 1nnm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PG4 OCA].
 
==Reference==
The 1.75 A crystal structure of acetyl-CoA synthetase bound to adenosine-5'-propylphosphate and coenzyme A., Gulick AM, Starai VJ, Horswill AR, Homick KM, Escalante-Semerena JC, Biochemistry. 2003 Mar 18;42(10):2866-73. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12627952 12627952]
[[Category: Acetate--CoA ligase]]
[[Category: Salmonella enterica]]
[[Category: Salmonella enterica]]
[[Category: Single protein]]
[[Category: Escalante-Semerena JC]]
[[Category: Escalante-Semerena, J C.]]
[[Category: Gulick AM]]
[[Category: Gulick, A M.]]
[[Category: Homick KM]]
[[Category: Homick, K M.]]
[[Category: Horswill AR]]
[[Category: Horswill, A R.]]
[[Category: Starai VJ]]
[[Category: Starai, V J.]]
[[Category: Adenylate-forming]]
[[Category: Amp-forming]]
[[Category: Thioester-forming]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:37:09 2008''

Latest revision as of 11:07, 14 February 2024

Acetyl CoA Synthetase, Salmonella entericaAcetyl CoA Synthetase, Salmonella enterica

Structural highlights

1pg4 is a 2 chain structure with sequence from Salmonella enterica. This structure supersedes the now removed PDB entry 1nnm. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.75Å
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

1pg4, resolution 1.75Å

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