2cdh: Difference between revisions

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[[Image:2cdh.gif|left|200px]]


{{Structure
==ARCHITECTURE OF THE THERMOMYCES LANUGINOSUS FUNGAL FATTY ACID SYNTHASE AT 5 ANGSTROM RESOLUTION.==
|PDB= 2cdh |SIZE=350|CAPTION= <scene name='initialview01'>2cdh</scene>, resolution 4.20&Aring;
<StructureSection load='2cdh' size='340' side='right'caption='[[2cdh]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
|SITE=
== Structural highlights ==
|LIGAND=
<table><tr><td colspan='2'>[[2cdh]] is a 36 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermomyces_lanuginosus Thermomyces lanuginosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CDH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CDH FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.2&#8491;</td></tr>
|GENE=  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2cdh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cdh OCA], [https://pdbe.org/2cdh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cdh RCSB], [https://www.ebi.ac.uk/pdbsum/2cdh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cdh ProSAT]</span></td></tr>
}}
</table>
 
== Function ==
'''ARCHITECTURE OF THE THERMOMYCES LANUGINOSUS FUNGAL FATTY ACID SYNTHASE AT 5 ANGSTROM RESOLUTION.'''
[https://www.uniprot.org/uniprot/FABB_ECOLI FABB_ECOLI] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Specific for elongation from C-10 to unsaturated C-16 and C-18 fatty acids.
 
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
==Overview==
Check<jmol>
All steps of fatty acid synthesis in fungi are catalyzed by the fatty acid synthase, which forms a 2.6-megadalton alpha6beta6 complex. We have determined the molecular architecture of this multienzyme by fitting the structures of homologous enzymes that catalyze the individual steps of the reaction pathway into a 5 angstrom x-ray crystallographic electron density map. The huge assembly contains two separated reaction chambers, each equipped with three sets of active sites separated by distances up to approximately 130 angstroms, across which acyl carrier protein shuttles substrates during the reaction cycle. Regions of the electron density arising from well-defined structural features outside the catalytic domains separate the two reaction chambers and serve as a matrix in which domains carrying the various active sites are embedded. The structure rationalizes the compartmentalization of fatty acid synthesis, and the spatial arrangement of the active sites has specific implications for our understanding of the reaction cycle mechanism and of the architecture of multienzymes in general.
  <jmolCheckbox>
 
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cd/2cdh_consurf.spt"</scriptWhenChecked>
==About this Structure==
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
2CDH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermomyces_lanuginosus Thermomyces lanuginosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CDH OCA].  
    <text>to colour the structure by Evolutionary Conservation</text>
 
  </jmolCheckbox>
==Reference==
</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=2cdh ConSurf].
Architecture of a fungal fatty acid synthase at 5 A resolution., Jenni S, Leibundgut M, Maier T, Ban N, Science. 2006 Mar 3;311(5765):1263-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16513976 16513976]
<div style="clear:both"></div>
[[Category: Single protein]]
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermomyces lanuginosus]]
[[Category: Thermomyces lanuginosus]]
[[Category: Ban, N.]]
[[Category: Ban N]]
[[Category: Jenni, S.]]
[[Category: Jenni S]]
[[Category: Leibundgut, M.]]
[[Category: Leibundgut M]]
[[Category: Maier, T.]]
[[Category: Maier T]]
[[Category: fatty acid synthesis]]
[[Category: fungal fatty acid synthase]]
[[Category: multifunctional enzyme]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:14:04 2008''

Latest revision as of 12:17, 14 February 2024

ARCHITECTURE OF THE THERMOMYCES LANUGINOSUS FUNGAL FATTY ACID SYNTHASE AT 5 ANGSTROM RESOLUTION.ARCHITECTURE OF THE THERMOMYCES LANUGINOSUS FUNGAL FATTY ACID SYNTHASE AT 5 ANGSTROM RESOLUTION.

Structural highlights

2cdh is a 36 chain structure with sequence from Thermomyces lanuginosus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 4.2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FABB_ECOLI Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Specific for elongation from C-10 to unsaturated C-16 and C-18 fatty acids.

Evolutionary Conservation

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

2cdh, resolution 4.20Å

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