2v9e: Difference between revisions

Revision as of 17:29, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2v9e.png

Template:STRUCTURE 2v9e

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

Template:ABSTRACT PUBMED 18187656

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

Structure and catalytic mechanism of L-rhamnulose-1-phosphate aldolase., Kroemer M, Merkel I, Schulz GE, Biochemistry. 2003 Sep 16;42(36):10560-8. PMID:12962479

Page seeded by OCA on Sun Jul 27 17:29:36 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_2v9e|  PDB=2v9e  |  SCENE=  }}
-'''L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E192A-K248W-A273S)'''
+===L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E192A-K248W-A273S)===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_18187656}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18187656 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18187656}}
 ==About this Structure==
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 ==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://www.ncbi.nlm.nih.gov/pubmed/18187656 18187656]
+Structure and catalytic mechanism of L-rhamnulose-1-phosphate aldolase., Kroemer M, Merkel I, Schulz GE, Biochemistry. 2003 Sep 16;42(36):10560-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12962479 12962479]
 [[Category: Escherichia coli]]
 [[Category: Rhamnulose-1-phosphate aldolase]]
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 [[Category: Zinc]]
 [[Category: Zinc enzyme]]
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