2v9m

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (15:11, 13 December 2023) (edit) (undo)
 
(7 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2v9m.png|left|200px]]
 
-
{{STRUCTURE_2v9m| PDB=2v9m | SCENE= }}
+
==L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT A87M- T109F-E192A)==
 +
<StructureSection load='2v9m' size='340' side='right'caption='[[2v9m]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2v9m]] 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=2V9M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V9M FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=2v9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v9m OCA], [https://pdbe.org/2v9m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v9m RCSB], [https://www.ebi.ac.uk/pdbsum/2v9m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v9m ProSAT]</span></td></tr>
 +
</table>
 +
== 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/v9/2v9m_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=2v9m 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 A87M-T109F-E192A)===
+
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>
-
{{ABSTRACT_PUBMED_18187656}}
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
==About this Structure==
+
<div class="pdbe-citations 2v9m" style="background-color:#fffaf0;"></div>
-
[[2v9m]] is a 2 chain structure of [[Aldolase]] with 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=2V9M OCA].
+
==See Also==
==See Also==
-
*[[Aldolase|Aldolase]]
+
*[[Aldolase 3D structures|Aldolase 3D structures]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
<ref group="xtra">PMID:018187656</ref><ref group="xtra">PMID:012962479</ref><references group="xtra"/>
+
__TOC__
 +
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Rhamnulose-1-phosphate aldolase]]
+
[[Category: Large Structures]]
-
[[Category: Grueninger, D.]]
+
[[Category: Grueninger D]]
-
[[Category: Schulz, G E.]]
+
[[Category: Schulz GE]]
-
[[Category: 2-ketose degradation]]
+
-
[[Category: Aggregation]]
+
-
[[Category: Aldolase]]
+
-
[[Category: Class ii]]
+
-
[[Category: Cleavage of l-rhamnulose-1-phosphate to dihydroxyacetoneph bacterial l-rhamnose metabolism]]
+
-
[[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 enzyme]]
+

Current revision

L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT A87M- T109F-E192A)

PDB ID 2v9m

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools