2v9e: Difference between revisions
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[[Image:2v9e.jpg|left|200px]] | [[Image:2v9e.jpg|left|200px]] | ||
'''L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E192A-K248W-A273S)''' | {{Structure | ||
|PDB= 2v9e |SIZE=350|CAPTION= <scene name='initialview01'>2v9e</scene>, resolution 1.58Å | |||
|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> | |||
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=ACT:ACETATE ION'>ACT</scene> | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E192A-K248W-A273S)''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2V9E is a [ | 2V9E 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]. | ||
==Reference== | ==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:// | 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: Escherichia coli]] | ||
[[Category: Rhamnulose-1-phosphate aldolase]] | [[Category: Rhamnulose-1-phosphate aldolase]] | ||
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[[Category: zinc enzyme]] | [[Category: zinc enzyme]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:44:30 2008'' |
Revision as of 19:44, 20 March 2008
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, resolution 1.58Å | |||||||
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Sites: | , , , , , , , , , and | ||||||
Ligands: | and | ||||||
Activity: | Rhamnulose-1-phosphate aldolase, with EC number 4.1.2.19 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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 Thu Mar 20 18:44:30 2008
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- Escherichia coli
- Rhamnulose-1-phosphate aldolase
- Single protein
- Grueninger, D.
- Schulz, G E.
- ACT
- ZN
- 2-ketose degradation
- Aggregation
- Aldolase
- Bacterial l-rhamnose metabolism
- Class ii
- Cleavage of l-rhamnulose-1-phosphate to dihydroxyacetone
- Cytoplasm
- Entropy index
- Fibrillation
- Interface design
- Lyase
- Metal-binding
- Oligomerization
- Protein engineering
- Protein-protein interface
- Rare sugar
- Rhamnose metabolism
- Surface mutation
- Zinc
- Zinc enzyme