2uyv: Difference between revisions

Revision as of 19:51, 21 February 2008

L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT Q6Y-E192A)

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

Page seeded by OCA on Thu Feb 21 18:51:49 2008

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OCA

@@ Line 4: / Line 4: @@
 ==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 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 Structure==
-UYV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=TLA:'>TLA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Sites: <scene name='pdbsite=AC1:Tla Binding Site For Chain A'>AC1</scene>, <scene name='pdbsite=AC2:Tla Binding Site For Chain B'>AC2</scene>, <scene name='pdbsite=AC3:Tla Binding Site For Chain C'>AC3</scene>, <scene name='pdbsite=AC4:Tla Binding Site For Chain D'>AC4</scene>, <scene name='pdbsite=AC5:Zn Binding Site For Chain A'>AC5</scene>, <scene name='pdbsite=AC6:Zn Binding Site For Chain B'>AC6</scene>, <scene name='pdbsite=AC7:Zn Binding Site For Chain C'>AC7</scene>, <scene name='pdbsite=AC8:Zn Binding Site For Chain D'>AC8</scene> and <scene name='pdbsite=AC9:Tla Binding Site For Chain A'>AC9</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UYV OCA].
+UYV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=TLA:'>TLA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Sites: <scene name='pdbsite=AC1:Tla+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Tla+Binding+Site+For+Chain+B'>AC2</scene>, <scene name='pdbsite=AC3:Tla+Binding+Site+For+Chain+C'>AC3</scene>, <scene name='pdbsite=AC4:Tla+Binding+Site+For+Chain+D'>AC4</scene>, <scene name='pdbsite=AC5:Zn+Binding+Site+For+Chain+A'>AC5</scene>, <scene name='pdbsite=AC6:Zn+Binding+Site+For+Chain+B'>AC6</scene>, <scene name='pdbsite=AC7:Zn+Binding+Site+For+Chain+C'>AC7</scene>, <scene name='pdbsite=AC8:Zn+Binding+Site+For+Chain+D'>AC8</scene> and <scene name='pdbsite=AC9:Tla+Binding+Site+For+Chain+A'>AC9</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UYV OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Single protein]]
 [[Category: Grueninger, D.]]
-[[Category: Schulz, G.E.]]
+[[Category: Schulz, G E.]]
 [[Category: TLA]]
 [[Category: ZN]]
@@ Line 36: / Line 36: @@
 [[Category: zinc enzyme]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 10:45:02 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:51:49 2008''