2uyv: Difference between revisions
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==L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT Q6Y-E192A)== | ==L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT Q6Y- E192A)== | ||
<StructureSection load='2uyv' size='340' side='right' caption='[[2uyv]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='2uyv' size='340' side='right' caption='[[2uyv]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uy/2uyv_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uy/2uyv_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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[[Category: Rhamnose metabolism]] | [[Category: Rhamnose metabolism]] | ||
[[Category: Surface mutation]] | [[Category: Surface mutation]] | ||
[[Category: Zinc]] | |||
[[Category: Zinc enzyme]] | [[Category: Zinc enzyme]] | ||
Revision as of 12:02, 12 September 2018
L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT Q6Y- E192A)L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT Q6Y- E192A)
Structural highlights
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 PubMedThe 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 AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Bacillus coli migula 1895
- Rhamnulose-1-phosphate aldolase
- Grueninger, D
- Schulz, G E
- 2-ketose degradation
- Aggregation
- Aldolase
- Class ii
- Cleavage of l-rhamnulose-1-phosphate to dihydroxyacetoneph bacterial l-rhamnose metabolism
- Fibrillation
- Interface design
- Lyase
- Metal-binding
- Oligomerization
- Protein engineering
- Protein-protein interface
- Rare sugar
- Rhamnose metabolism
- Surface mutation
- Zinc
- Zinc enzyme