2v2a

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:2v2a.jpg|left|200px]]
[[Image:2v2a.jpg|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 2v2a |SIZE=350|CAPTION= <scene name='initialview01'>2v2a</scene>, resolution 1.75&Aring;
+
The line below this paragraph, containing "STRUCTURE_2v2a", creates the "Structure Box" on the page.
-
|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> and <scene name='pdbsite=AC3:13p+Binding+Site+For+Chain+A'>AC3</scene>
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND= <scene name='pdbligand=13P:1,3-DIHYDROXYACETONEPHOSPHATE'>13P</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY= <span class='plainlinks'>[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] </span>
+
or leave the SCENE parameter empty for the default display.
-
|GENE=
+
-->
-
|DOMAIN=
+
{{STRUCTURE_2v2a| PDB=2v2a | SCENE= }}
-
|RELATEDENTRY=[[1gt7|1GT7]], [[1ojr|1OJR]], [[2uyu|2UYU]], [[2uyv|2UYV]], [[2v29|2V29]], [[2v2b|2V2B]]
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v2a OCA], [http://www.ebi.ac.uk/pdbsum/2v2a PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2v2a RCSB]</span>
+
-
}}
+
'''L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E192A-K248G-R253A-E254A)'''
'''L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E192A-K248G-R253A-E254A)'''
Line 29: Line 26:
[[Category: Schulz, G E.]]
[[Category: Schulz, G E.]]
[[Category: 2-ketose degradation]]
[[Category: 2-ketose degradation]]
-
[[Category: aldolase]]
+
[[Category: Aldolase]]
-
[[Category: bacterial l-rhamnose metabolism]]
+
[[Category: Bacterial l-rhamnose metabolism]]
-
[[Category: class ii]]
+
[[Category: Class ii]]
-
[[Category: cleavage of l-rhamnulose-1-phosphate to dihydroxyacetone phosphate]]
+
[[Category: Cleavage of l-rhamnulose-1-phosphate to dihydroxyacetone phosphate]]
-
[[Category: domain motion for mechanical support of catalysis]]
+
[[Category: Domain motion for mechanical support of catalysis]]
-
[[Category: lyase]]
+
[[Category: Lyase]]
-
[[Category: metal-binding]]
+
[[Category: Metal-binding]]
-
[[Category: protein engineering]]
+
[[Category: Protein engineering]]
-
[[Category: protein-protein interface]]
+
[[Category: Protein-protein interface]]
-
[[Category: rare sugar]]
+
[[Category: Rare sugar]]
-
[[Category: rhamnose metabolism]]
+
[[Category: Rhamnose metabolism]]
-
[[Category: surface mutation]]
+
[[Category: Surface mutation]]
-
[[Category: zinc]]
+
[[Category: Zinc]]
-
[[Category: zinc enzyme]]
+
[[Category: Zinc enzyme]]
-
 
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:05:20 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:07:48 2008''
+

Revision as of 15:05, 4 May 2008

Image:2v2a.jpg

Template:STRUCTURE 2v2a

L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E192A-K248G-R253A-E254A)


Overview

The enzyme l-rhamnulose-1-phosphate aldolase from Escherichia coli participates in the degradation pathway of l-rhamnose, a ubiquitous deoxy-hexose. It is a homotetramer of the rare C4-symmetric type with N-terminal domains protruding like antennas from the main body. A mobility analysis of the enzyme gave rise to the hypothesis that an anisotropic thermal antenna motion may support the catalysis (Kroemer et al., Biochemistry 42, 10560, 2003). We checked this hypothesis by generating four single mutants and one disulfide bridge that were designed to reduce the mobility of the antenna domain without disturbing the chain-fold or the active center. The catalytic rates of the mutants revealed activity reductions that correlated well with the expected antenna fixation. Among these mutants, K15W was crystallized, structurally elucidated, and used as a guide for modeling the others. The structure confirmed the design because the mutation introduced a tight nonpolar contact to a neighboring subunit that fixed the antenna but did not affect the main chain. The fixation was confirmed by a comparison of the anisotropic B-factors describing the mobility of the domains. It turned out that the distinctly anisotropic mobility of the wild-type antenna domain has become isotropic in K15W, in agreement with the design. We suggest that, like K15W, the other mutations also followed the design, validating the correlation between antenna mobility and activity. This correlation suggests that the domain mobility facilitates the reaction.

About this Structure

2V2A is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Antenna domain mobility and enzymatic reaction of L-rhamnulose-1-phosphate aldolase., Grueninger D, Schulz GE, Biochemistry. 2008 Jan 15;47(2):607-14. Epub 2007 Dec 18. PMID:18085797 Page seeded by OCA on Sun May 4 18:05:20 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2v2a"
Personal tools