2v9f

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{{Seed}}
 
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[[Image:2v9f.png|left|200px]]
 
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==L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E192A- K248W-A273S)==
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The line below this paragraph, containing "STRUCTURE_2v9f", creates the "Structure Box" on the page.
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<StructureSection load='2v9f' size='340' side='right'caption='[[2v9f]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2v9f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V9F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V9F FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_2v9f| PDB=2v9f | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2v9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v9f OCA], [https://pdbe.org/2v9f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v9f RCSB], [https://www.ebi.ac.uk/pdbsum/2v9f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v9f ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RHAD_ECOLI RHAD_ECOLI] Catalyzes the reversible cleavage of L-rhamnulose-1-phosphate to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde.[HAMAP-Rule:MF_00770]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v9/2v9f_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2v9f ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The analysis of natural contact interfaces between protein subunits and between proteins has disclosed some general rules governing their association. We have applied these rules to produce a number of novel assemblies, demonstrating that a given protein can be engineered to form contacts at various points of its surface. Symmetry plays an important role because it defines the multiplicity of a designed contact and therefore the number of required mutations. Some of the proteins needed only a single side-chain alteration in order to associate to a higher-order complex. The mobility of the buried side chains has to be taken into account. Four assemblies have been structurally elucidated. Comparisons between the designed contacts and the results will provide useful guidelines for the development of future architectures.
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===L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E192A-K248W-A273S)===
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Designed protein-protein association.,Grueninger D, Treiber N, Ziegler MO, Koetter JW, Schulze MS, Schulz GE Science. 2008 Jan 11;319(5860):206-9. PMID:18187656<ref>PMID:18187656</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2v9f" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_18187656}}, adds the Publication Abstract to the page
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*[[Aldolase 3D structures|Aldolase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 18187656 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18187656}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2V9F is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V9F OCA].
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==Reference==
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<ref group="xtra">PMID:18187656</ref><ref group="xtra">PMID:12962479</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Rhamnulose-1-phosphate aldolase]]
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[[Category: Large Structures]]
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[[Category: Grueninger, D.]]
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[[Category: Grueninger D]]
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[[Category: Schulz, G E.]]
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[[Category: Schulz GE]]
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[[Category: 2-ketose degradation]]
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[[Category: Aggregation]]
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[[Category: Aldolase]]
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[[Category: Class ii]]
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[[Category: Cleavage of l-rhamnulose-1-phosphate to dihydroxyacetoneph bacterial l-rhamnose metabolism]]
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[[Category: Cytoplasm]]
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[[Category: Entropy index]]
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[[Category: Fibrillation]]
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[[Category: Interface design]]
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[[Category: Lyase]]
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[[Category: Metal-binding]]
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[[Category: Oligomerization]]
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[[Category: Protein engineering]]
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[[Category: Protein-protein interface]]
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[[Category: Rare sugar]]
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[[Category: Rhamnose metabolism]]
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[[Category: Surface mutation]]
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[[Category: Zinc]]
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[[Category: Zinc enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 10:05:55 2009''
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Current revision

L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E192A- K248W-A273S)

PDB ID 2v9f

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