2v9e: Difference between revisions

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[[Image:2v9e.jpg|left|200px]]
[[Image:2v9e.jpg|left|200px]]


{{Structure
<!--
|PDB= 2v9e |SIZE=350|CAPTION= <scene name='initialview01'>2v9e</scene>, resolution 1.58&Aring;
The line below this paragraph, containing "STRUCTURE_2v9e", creates the "Structure Box" on the page.
|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>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|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>
or leave the SCENE parameter empty for the default display.
|GENE=  
-->
|DOMAIN=
{{STRUCTURE_2v9e| PDB=2v9e  | SCENE= }}  
|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]]
|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>
}}


'''L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E192A-K248W-A273S)'''
'''L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E192A-K248W-A273S)'''
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[[Category: Schulz, G E.]]
[[Category: Schulz, G E.]]
[[Category: 2-ketose degradation]]
[[Category: 2-ketose degradation]]
[[Category: aggregation]]
[[Category: Aggregation]]
[[Category: aldolase]]
[[Category: Aldolase]]
[[Category: bacterial l-rhamnose metabolism]]
[[Category: Bacterial l-rhamnose metabolism]]
[[Category: class ii]]
[[Category: Class ii]]
[[Category: cleavage of l-rhamnulose-1-phosphate to dihydroxyacetone]]
[[Category: Cleavage of l-rhamnulose-1-phosphate to dihydroxyacetone]]
[[Category: cytoplasm]]
[[Category: Cytoplasm]]
[[Category: entropy index]]
[[Category: Entropy index]]
[[Category: fibrillation]]
[[Category: Fibrillation]]
[[Category: interface design]]
[[Category: Interface design]]
[[Category: lyase]]
[[Category: Lyase]]
[[Category: metal-binding]]
[[Category: Metal-binding]]
[[Category: oligomerization]]
[[Category: Oligomerization]]
[[Category: protein engineering]]
[[Category: Protein engineering]]
[[Category: protein-protein interface]]
[[Category: Protein-protein interface]]
[[Category: rare sugar]]
[[Category: Rare sugar]]
[[Category: rhamnose metabolism]]
[[Category: Rhamnose metabolism]]
[[Category: surface mutation]]
[[Category: Surface mutation]]
[[Category: zinc]]
[[Category: Zinc]]
[[Category: zinc enzyme]]
[[Category: Zinc enzyme]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 18:25:29 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:09:59 2008''

Revision as of 18:25, 4 May 2008

File:2v9e.jpg

Template:STRUCTURE 2v9e

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


OverviewOverview

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.

About this StructureAbout this Structure

2V9E is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

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 Page seeded by OCA on Sun May 4 18:25:29 2008

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