2a7s: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(9 intermediate revisions by the same user not shown)
Line 1: Line 1:
{{Seed}}
[[Image:2a7s.png|left|200px]]


<!--
==Crystal Structure of the Acyl-CoA Carboxylase, AccD5, from Mycobacterium tuberculosis==
The line below this paragraph, containing "STRUCTURE_2a7s", creates the "Structure Box" on the page.
<StructureSection load='2a7s' size='340' side='right'caption='[[2a7s]], [[Resolution|resolution]] 2.90&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'>[[2a7s]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A7S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A7S 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]] 2.9&#8491;</td></tr>
-->
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2a7s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a7s OCA], [https://pdbe.org/2a7s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a7s RCSB], [https://www.ebi.ac.uk/pdbsum/2a7s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a7s ProSAT]</span></td></tr>
{{STRUCTURE_2a7s|  PDB=2a7s  |  SCENE=  }}
</table>
 
== Function ==
===Crystal Structure of the Acyl-CoA Carboxylase, AccD5, from Mycobacterium tuberculosis===
[https://www.uniprot.org/uniprot/ACCD5_MYCTU ACCD5_MYCTU] Component of a biotin-dependent acyl-CoA carboxylase complex. This subunit transfers the CO2 from carboxybiotin to the CoA ester substrate (PubMed:16354663, PubMed:16385038, PubMed:28222482). When associated with the alpha3 subunit AccA3, is involved in the carboxylation of acetyl-CoA and propionyl-CoA, with a preference for propionyl-CoA (PubMed:16354663, PubMed:16385038, PubMed:28222482). Is also required for the activity of the long-chain acyl-CoA carboxylase (LCC) complex (PubMed:28222482).<ref>PMID:16354663</ref> <ref>PMID:16385038</ref> <ref>PMID:28222482</ref>
 
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
<!--
Check<jmol>
The line below this paragraph, {{ABSTRACT_PUBMED_16492739}}, adds the Publication Abstract to the page
  <jmolCheckbox>
(as it appears on PubMed at http://www.pubmed.gov), where 16492739 is the PubMed ID number.
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a7/2a7s_consurf.spt"</scriptWhenChecked>
-->
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
{{ABSTRACT_PUBMED_16492739}}
    <text>to colour the structure by Evolutionary Conservation</text>
 
  </jmolCheckbox>
==About this Structure==
</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=2a7s ConSurf].
2A7S is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A7S OCA].  
<div style="clear:both"></div>
 
== References ==
==Reference==
<references/>
Structure-based inhibitor design of AccD5, an essential acyl-CoA carboxylase carboxyltransferase domain of Mycobacterium tuberculosis., Lin TW, Melgar MM, Kurth D, Swamidass SJ, Purdon J, Tseng T, Gago G, Baldi P, Gramajo H, Tsai SC, Proc Natl Acad Sci U S A. 2006 Feb 28;103(9):3072-7. Epub 2006 Feb 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16492739 16492739]
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Propionyl-CoA carboxylase]]
[[Category: Lin T]]
[[Category: Single protein]]
[[Category: Melgar M]]
[[Category: Lin, T.]]
[[Category: Purdon J]]
[[Category: Melgar, M.]]
[[Category: Tsai SC]]
[[Category: Purdon, J.]]
[[Category: Tseng T]]
[[Category: Tsai, S C.]]
[[Category: Tseng, T.]]
[[Category: Acetyl-coa carboxylase]]
[[Category: Acyl-coa carboxylase]]
[[Category: Carboxylase]]
[[Category: Carboxyltransferase]]
[[Category: Fatty acid]]
[[Category: Mycolic acid]]
[[Category: Polyketide]]
[[Category: Propionyl-coa carboxylase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:36:26 2008''

Latest revision as of 12:11, 14 February 2024

Crystal Structure of the Acyl-CoA Carboxylase, AccD5, from Mycobacterium tuberculosisCrystal Structure of the Acyl-CoA Carboxylase, AccD5, from Mycobacterium tuberculosis

Structural highlights

2a7s is a 6 chain structure with sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.9Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ACCD5_MYCTU Component of a biotin-dependent acyl-CoA carboxylase complex. This subunit transfers the CO2 from carboxybiotin to the CoA ester substrate (PubMed:16354663, PubMed:16385038, PubMed:28222482). When associated with the alpha3 subunit AccA3, is involved in the carboxylation of acetyl-CoA and propionyl-CoA, with a preference for propionyl-CoA (PubMed:16354663, PubMed:16385038, PubMed:28222482). Is also required for the activity of the long-chain acyl-CoA carboxylase (LCC) complex (PubMed:28222482).[1] [2] [3]

Evolutionary Conservation

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

References

  1. ↑ Oh TJ, Daniel J, Kim HJ, Sirakova TD, Kolattukudy PE. Identification and characterization of Rv3281 as a novel subunit of a biotin-dependent acyl-CoA Carboxylase in Mycobacterium tuberculosis H37Rv. J Biol Chem. 2006 Feb 17;281(7):3899-908. PMID:16354663 doi:10.1074/jbc.M511761200
  2. ↑ Gago G, Kurth D, Diacovich L, Tsai SC, Gramajo H. Biochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis. J Bacteriol. 2006 Jan;188(2):477-86. PMID:16385038 doi:10.1128/JB.188.2.477-486.2006
  3. ↑ Bazet Lyonnet B, Diacovich L, Gago G, Spina L, Bardou F, Lemassu A, Quémard A, Gramajo H. Functional reconstitution of the Mycobacterium tuberculosis long-chain acyl-CoA carboxylase from multiple acyl-CoA subunits. FEBS J. 2017 Apr;284(7):1110-1125. PMID:28222482 doi:10.1111/febs.14046

2a7s, resolution 2.90Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=2a7s&oldid=4057644"