2v9e: Difference between revisions

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-[[Image:2v9e.jpg|left|200px]]
- {{Structure
+==L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E192A- K248W-A273S)==
-|PDB= 2v9e |SIZE=350|CAPTION= <scene name='initialview01'>2v9e</scene>, resolution 1.58&Aring;
+<StructureSection load='2v9e' size='340' side='right'caption='[[2v9e]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
-|SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Zn+Binding+Site+For+Chain+A'>AC2</scene>, <scene name='pdbsite=AC3:Zn+Binding+Site+For+Chain+A'>AC3</scene>, <scene name='pdbsite=AC4:Zn+Binding+Site+For+Chain+B'>AC4</scene>, <scene name='pdbsite=AC5:Zn+Binding+Site+For+Chain+B'>AC5</scene>, <scene name='pdbsite=AC6:Zn+Binding+Site+For+Chain+B'>AC6</scene>, <scene name='pdbsite=AC7:Act+Binding+Site+For+Chain+A'>AC7</scene>, <scene name='pdbsite=AC8:Act+Binding+Site+For+Chain+A'>AC8</scene>, <scene name='pdbsite=AC9:Act+Binding+Site+For+Chain+A'>AC9</scene>, <scene name='pdbsite=BC1:Act+Binding+Site+For+Chain+A'>BC1</scene> and <scene name='pdbsite=BC2:Act+Binding+Site+For+Chain+B'>BC2</scene>
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
+<table><tr><td colspan='2'>[[2v9e]] is a 2 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=2V9E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V9E FirstGlance]. <br>
-|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Rhamnulose-1-phosphate_aldolase Rhamnulose-1-phosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.19 4.1.2.19] </span>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.58&#8491;</td></tr>
-|GENE=
+<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>
-|DOMAIN=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2v9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v9e OCA], [https://pdbe.org/2v9e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v9e RCSB], [https://www.ebi.ac.uk/pdbsum/2v9e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v9e ProSAT]</span></td></tr>
-|RELATEDENTRY=[[1gt7|1GT7]], [[1ojr|1OJR]], [[2uyu|2UYU]], [[2v2b|2V2B]], [[2uyv|2UYV]], [[2v29|2V29]], [[2v2a|2V2A]], [[2v9f|2V9F]], [[2v9g|2V9G]], [[2v9i|2V9I]], [[2v9l|2V9L]], [[2v9m|2V9M]]
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v9e OCA], [http://www.ebi.ac.uk/pdbsum/2v9e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2v9e RCSB]</span>
+== Function ==
-}}
+[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]
+== 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/v9/2v9e_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=2v9e ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-'''L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E192A-K248W-A273S)'''
+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>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2v9e" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-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.
+*[[Aldolase 3D structures|Aldolase 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-V9E is a [[Single protein]] 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=2V9E OCA].
+__TOC__
+</StructureSection>
-==Reference==
-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:[http://www.ncbi.nlm.nih.gov/pubmed/18187656 18187656]
 [[Category: Escherichia coli]]
-[[Category: Rhamnulose-1-phosphate aldolase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Grueninger D]]
-[[Category: Grueninger, D.]]
+[[Category: Schulz GE]]
-[[Category: Schulz, G E.]]
-[[Category: 2-ketose degradation]]
-[[Category: aggregation]]
-[[Category: aldolase]]
-[[Category: bacterial l-rhamnose metabolism]]
-[[Category: class ii]]
-[[Category: cleavage of l-rhamnulose-1-phosphate to dihydroxyacetone]]
-[[Category: cytoplasm]]
-[[Category: entropy index]]
-[[Category: fibrillation]]
-[[Category: interface design]]
-[[Category: lyase]]
-[[Category: metal-binding]]
-[[Category: oligomerization]]
-[[Category: protein engineering]]
-[[Category: protein-protein interface]]
-[[Category: rare sugar]]
-[[Category: rhamnose metabolism]]
-[[Category: surface mutation]]
-[[Category: zinc]]
-[[Category: zinc enzyme]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:09:59 2008''