2uyv

Revision as of 11:45, 23 January 2008 by OCA (talk | contribs) (New page: left|200px<br /><applet load="2uyv" size="350" color="white" frame="true" align="right" spinBox="true" caption="2uyv, resolution 2.2Å" /> '''L-RHAMNULOSE-1-PHOSPH...)
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L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT Q6Y-E192A)

File:2uyv.jpg


2uyv, resolution 2.2Å

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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

2UYV is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as Rhamnulose-1-phosphate aldolase, with EC number 4.1.2.19 Known structural/functional Sites: , , , , , , , and . 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

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