1a59: Difference between revisions

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[[Image:1a59.png|left|200px]]


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==COLD-ACTIVE CITRATE SYNTHASE==
The line below this paragraph, containing "STRUCTURE_1a59", creates the "Structure Box" on the page.
<StructureSection load='1a59' size='340' side='right'caption='[[1a59]], [[Resolution|resolution]] 2.09&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'>[[1a59]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Antarctic_bacterium_DS2-3R Antarctic bacterium DS2-3R]. The September 2007 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Citrate Synthase''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2007_9 10.2210/rcsb_pdb/mom_2007_9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A59 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]] 2.09&#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=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr>
{{STRUCTURE_1a59| PDB=1a59 |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a59 OCA], [https://pdbe.org/1a59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a59 RCSB], [https://www.ebi.ac.uk/pdbsum/1a59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a59 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PRPC_ABDS2 PRPC_ABDS2] Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield 2-methylcitrate (2-MC) and CoA. Also catalyzes the condensation of oxaloacetate with acetyl-CoA but with a lower specificity.<ref>PMID:9310359</ref> <ref>PMID:9579066</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/a5/1a59_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=1a59 ConSurf].
<div style="clear:both"></div>


===COLD-ACTIVE CITRATE SYNTHASE===
==See Also==
 
*[[Citrate Synthase 3D structures|Citrate Synthase 3D structures]]
 
== References ==
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[[Category: Antarctic bacterium DS2-3R]]
{{ABSTRACT_PUBMED_9551556}}
 
==About this Structure==
[[1a59]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacteria Bacteria]. The September 2007 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Citrate Synthase''  by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2007_9 10.2210/rcsb_pdb/mom_2007_9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A59 OCA].
 
==Reference==
<ref group="xtra">PMID:009551556</ref><ref group="xtra">PMID:014997520</ref><references group="xtra"/>
[[Category: Bacteria]]
[[Category: Citrate Synthase]]
[[Category: Citrate Synthase]]
[[Category: Large Structures]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Danson, M J.]]
[[Category: Danson MJ]]
[[Category: Gerike, U.]]
[[Category: Gerike U]]
[[Category: Hough, D W.]]
[[Category: Hough DW]]
[[Category: Russell, R J.M.]]
[[Category: Russell RJM]]
[[Category: Taylor, G L.]]
[[Category: Taylor GL]]
[[Category: Cold-activity]]

Latest revision as of 09:27, 7 February 2024

COLD-ACTIVE CITRATE SYNTHASECOLD-ACTIVE CITRATE SYNTHASE

Structural highlights

1a59 is a 1 chain structure with sequence from Antarctic bacterium DS2-3R. The September 2007 RCSB PDB Molecule of the Month feature on Citrate Synthase by David S. Goodsell is 10.2210/rcsb_pdb/mom_2007_9. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.09Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PRPC_ABDS2 Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield 2-methylcitrate (2-MC) and CoA. Also catalyzes the condensation of oxaloacetate with acetyl-CoA but with a lower specificity.[1] [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. ↑ Gerike U, Danson MJ, Russell NJ, Hough DW. Sequencing and expression of the gene encoding a cold-active citrate synthase from an Antarctic bacterium, strain DS2-3R. Eur J Biochem. 1997 Aug 15;248(1):49-57. PMID:9310359 doi:10.1111/j.1432-1033.1997.00049.x
  2. ↑ Gerike U, Hough DW, Russell NJ, Dyall-Smith ML, Danson MJ. Citrate synthase and 2-methylcitrate synthase: structural, functional and evolutionary relationships. Microbiology (Reading). 1998 Apr;144 ( Pt 4):929-935. doi: , 10.1099/00221287-144-4-929. PMID:9579066 doi:http://dx.doi.org/10.1099/00221287-144-4-929

1a59, resolution 2.09Å

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