2v9e: Difference between revisions

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==L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E192A- K248W-A273S)==
==L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E192A- K248W-A273S)==
<StructureSection load='2v9e' size='340' side='right' caption='[[2v9e]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
<StructureSection load='2v9e' size='340' side='right'caption='[[2v9e]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2v9e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V9E FirstGlance]. <br>
<table><tr><td colspan='2'>[[2v9e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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 [http://proteopedia.org/fgij/fg.htm?mol=2V9E FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><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>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gt7|1gt7]], [[1ojr|1ojr]], [[2uyu|2uyu]], [[2v2b|2v2b]], [[2uyv|2uyv]], [[2v29|2v29]], [[2v2a|2v2a]], [[2v9f|2v9f]], [[2v9g|2v9g]], [[2v9i|2v9i]], [[2v9l|2v9l]], [[2v9m|2v9m]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gt7|1gt7]], [[1ojr|1ojr]], [[2uyu|2uyu]], [[2v2b|2v2b]], [[2uyv|2uyv]], [[2v29|2v29]], [[2v2a|2v2a]], [[2v9f|2v9f]], [[2v9g|2v9g]], [[2v9i|2v9i]], [[2v9l|2v9l]], [[2v9m|2v9m]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/2v9e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2v9e RCSB], [http://www.ebi.ac.uk/pdbsum/2v9e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2v9e ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2v9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v9e OCA], [http://pdbe.org/2v9e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2v9e RCSB], [http://www.ebi.ac.uk/pdbsum/2v9e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2v9e ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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==See Also==
==See Also==
*[[Aldolase|Aldolase]]
*[[Aldolase 3D structures|Aldolase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Bacillus coli migula 1895]]
[[Category: Large Structures]]
[[Category: Rhamnulose-1-phosphate aldolase]]
[[Category: Rhamnulose-1-phosphate aldolase]]
[[Category: Grueninger, D]]
[[Category: Grueninger, D]]

Revision as of 14:23, 17 June 2020

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

Structural highlights

2v9e is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Activity:Rhamnulose-1-phosphate aldolase, with EC number 4.1.2.19
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RHAD_ECOLI] Catalyzes the reversible cleavage of L-rhamnulose-1-phosphate to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde.[HAMAP-Rule:MF_00770]

Evolutionary Conservation

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

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Grueninger D, Treiber N, Ziegler MO, Koetter JW, Schulze MS, Schulz GE. Designed protein-protein association. Science. 2008 Jan 11;319(5860):206-9. PMID:18187656 doi:http://dx.doi.org/319/5860/206

2v9e, resolution 1.58Å

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