3fkr: Difference between revisions

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'''Unreleased structure'''


The entry 3fkr is ON HOLD  until Paper Publication
==Structure of L-2-keto-3-deoxyarabonate dehydratase complex with pyruvate==
 
<StructureSection load='3fkr' size='340' side='right'caption='[[3fkr]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
Authors: Shimada, N., Mikami, B.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[3fkr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_29145 Atcc 29145]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FKR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FKR FirstGlance]. <br>
Description: Structure of L-2-keto-3-deoxyarabonate dehydratase complex with pyruvate
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
 
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KPI:(2S)-2-AMINO-6-[(1-HYDROXY-1-OXO-PROPAN-2-YLIDENE)AMINO]HEXANOIC+ACID'>KPI</scene></td></tr>
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Sep  3 15:17:19 2009''
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3fkk|3fkk]]</div></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=3fkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fkr OCA], [https://pdbe.org/3fkr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fkr RCSB], [https://www.ebi.ac.uk/pdbsum/3fkr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fkr ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/KDADA_AZOBR KDADA_AZOBR]] Catalyzes the dehydration of L-2-keto-3-deoxyarabonate (L-KDA) to alpha-ketoglutaric semialdehyde (alphaKGSA). Is involved in a degradation pathway of L-arabinose that allows A.brasilense to grow on L-arabinose as a sole carbon source.<ref>PMID:16950779</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/fk/3fkr_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=3fkr ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Atcc 29145]]
[[Category: Large Structures]]
[[Category: Mikami, B]]
[[Category: Shimada, N]]
[[Category: Complex]]
[[Category: Dhdps/nal family]]
[[Category: Lyase]]
[[Category: Pyruvate]]

Latest revision as of 11:03, 2 March 2022

Structure of L-2-keto-3-deoxyarabonate dehydratase complex with pyruvateStructure of L-2-keto-3-deoxyarabonate dehydratase complex with pyruvate

Structural highlights

3fkr is a 2 chain structure with sequence from Atcc 29145. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
NonStd Res:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[KDADA_AZOBR] Catalyzes the dehydration of L-2-keto-3-deoxyarabonate (L-KDA) to alpha-ketoglutaric semialdehyde (alphaKGSA). Is involved in a degradation pathway of L-arabinose that allows A.brasilense to grow on L-arabinose as a sole carbon source.[1]

Evolutionary Conservation

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

References

  1. Watanabe S, Shimada N, Tajima K, Kodaki T, Makino K. Identification and characterization of L-arabonate dehydratase, L-2-keto-3-deoxyarabonate dehydratase, and L-arabinolactonase involved in an alternative pathway of L-arabinose metabolism. Novel evolutionary insight into sugar metabolism. J Biol Chem. 2006 Nov 3;281(44):33521-36. Epub 2006 Sep 1. PMID:16950779 doi:http://dx.doi.org/M606727200

3fkr, resolution 1.80Å

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