1zk2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1zk2.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1zk2.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1zk2| PDB=1zk2 | SCENE= }}
{{STRUCTURE_1zk2| PDB=1zk2 | SCENE= }}
-
'''Orthorhombic crystal structure of the apo-form of R-specific alcohol dehydrogenase (mutant G37D) from Lactobacillus brevis'''
+
===Orthorhombic crystal structure of the apo-form of R-specific alcohol dehydrogenase (mutant G37D) from Lactobacillus brevis===
-
==Overview==
+
<!--
-
The R-specific alcohol dehydrogenase (RADH) from Lactobacillus brevis is an NADP-dependent, homotetrameric member of the extended enzyme family of short-chain dehydrogenases/reductases (SDR) with a high biotechnological application potential. Its preferred in vitro substrates are prochiral ketones like acetophenone with almost invariably a small methyl group as one substituent and a bulky (often aromatic) moiety as the other. On the basis of an atomic-resolution structure of wild-type RADH in complex with NADP and acetophenone, we designed the mutant RADH-G37D, which should possess an improved cosubstrate specificity profile for biotechnological purposes, namely, a preference for NAD rather than NADP. Comparative kinetic measurements with wild-type and mutant RADH showed that this aim was achieved. To characterize the successful mutant structurally, we determined several, partly atomic-resolution, crystal structures of RADH-G37D both as an apo-enzyme and as ternary complex with NAD or NADH and phenylethanol. The increased affinity of RADH-G37D for NAD(H) depends on an interaction between the adenosine ribose moiety of NAD and the inserted aspartate side-chain. A structural comparison between RADH-G37D as apo-enzyme and as a part of a ternary complex revealed significant rearrangements of Ser141, Glu144, Tyr189 and Met205 in the vicinity of the active site. This plasticity contributes to generate a small hydrophobic pocket for the methyl group typical for RADH substrates, and a hydrophobic coat for the second, more variable and often aromatic, substituent. Around Ser141 we even found alternative conformations in the backbone. A structural adaptability in this region, which we describe here for the first time for an SDR enzyme, is probably functionally important, because it concerns Ser142, a member of the highly conserved catalytic tetrad typical for SDR enzymes. Moreover, it affects an extended proton relay system that has been identified recently as a critical element for the catalytic mechanism in SDR enzymes.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15896805}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15896805 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15896805}}
==About this Structure==
==About this Structure==
Line 20: Line 24:
==Reference==
==Reference==
Atomic resolution structures of R-specific alcohol dehydrogenase from Lactobacillus brevis provide the structural bases of its substrate and cosubstrate specificity., Schlieben NH, Niefind K, Muller J, Riebel B, Hummel W, Schomburg D, J Mol Biol. 2005 Jun 17;349(4):801-13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15896805 15896805]
Atomic resolution structures of R-specific alcohol dehydrogenase from Lactobacillus brevis provide the structural bases of its substrate and cosubstrate specificity., Schlieben NH, Niefind K, Muller J, Riebel B, Hummel W, Schomburg D, J Mol Biol. 2005 Jun 17;349(4):801-13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15896805 15896805]
 +
 +
The crystal structure of R-specific alcohol dehydrogenase from Lactobacillus brevis suggests the structural basis of its metal dependency., Niefind K, Muller J, Riebel B, Hummel W, Schomburg D, J Mol Biol. 2003 Mar 21;327(2):317-28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12628239 12628239]
 +
 +
Morphological study of allogeneic tumor growth in mice bearing a glass cylinder., Filippa DA, Dosne Pasqualini C, Medicina (B Aires). 1975 Jan-Feb;35(1):29-36. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1092950 1092950]
[[Category: Lactobacillus brevis]]
[[Category: Lactobacillus brevis]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 31: Line 39:
[[Category: R-specific alcohol dehydrogenase]]
[[Category: R-specific alcohol dehydrogenase]]
[[Category: Short chain reductases/dehydrogenase]]
[[Category: Short chain reductases/dehydrogenase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:43:10 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:41:10 2008''

Revision as of 04:41, 29 July 2008

Image:1zk2.png

Template:STRUCTURE 1zk2

Orthorhombic crystal structure of the apo-form of R-specific alcohol dehydrogenase (mutant G37D) from Lactobacillus brevis

Template:ABSTRACT PUBMED 15896805

About this Structure

1ZK2 is a Single protein structure of sequence from Lactobacillus brevis. Full crystallographic information is available from OCA.

Reference

Atomic resolution structures of R-specific alcohol dehydrogenase from Lactobacillus brevis provide the structural bases of its substrate and cosubstrate specificity., Schlieben NH, Niefind K, Muller J, Riebel B, Hummel W, Schomburg D, J Mol Biol. 2005 Jun 17;349(4):801-13. PMID:15896805

The crystal structure of R-specific alcohol dehydrogenase from Lactobacillus brevis suggests the structural basis of its metal dependency., Niefind K, Muller J, Riebel B, Hummel W, Schomburg D, J Mol Biol. 2003 Mar 21;327(2):317-28. PMID:12628239

Morphological study of allogeneic tumor growth in mice bearing a glass cylinder., Filippa DA, Dosne Pasqualini C, Medicina (B Aires). 1975 Jan-Feb;35(1):29-36. PMID:1092950

Page seeded by OCA on Tue Jul 29 07:41:10 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1zk2"
Personal tools