This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2v8g

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2v8g.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2v8g.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2v8g| PDB=2v8g | SCENE= }}
{{STRUCTURE_2v8g| PDB=2v8g | SCENE= }}
-
'''CRYSTAL STRUCTURE OF BETA-ALANINE SYNTHASE FROM SACCHAROMYCES KLUYVERI IN COMPLEX WITH THE PRODUCT BETA-ALANINE'''
+
===CRYSTAL STRUCTURE OF BETA-ALANINE SYNTHASE FROM SACCHAROMYCES KLUYVERI IN COMPLEX WITH THE PRODUCT BETA-ALANINE===
-
==Overview==
+
<!--
-
Beta-alanine synthase is the final enzyme of the reductive pyrimidine catabolic pathway, which is responsible for the breakdown of uracil and thymine in higher organisms. The fold of the homodimeric enzyme from the yeast Saccharomyces kluyveri identifies it as a member of the AcyI/M20 family of metallopeptidases. Its subunit consists of a catalytic domain harboring a di-zinc center and a smaller dimerization domain. The present site-directed mutagenesis studies identify Glu(159) and Arg(322) as crucial for catalysis and His(262) and His(397) as functionally important but not essential. We determined the crystal structures of wild-type beta-alanine synthase in complex with the reaction product beta-alanine, and of the mutant E159A with the substrate N-carbamyl-beta-alanine, revealing the closed state of a dimeric AcyI/M20 metallopeptidase-like enzyme. Subunit closure is achieved by a approximately 30 degrees rigid body domain rotation, which completes the active site by integration of substrate binding residues that belong to the dimerization domain of the same or the partner subunit. Substrate binding is achieved via a salt bridge, a number of hydrogen bonds, and coordination to one of the zinc ions of the di-metal center.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17916556}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17916556 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17916556}}
==About this Structure==
==About this Structure==
Line 20: Line 24:
==Reference==
==Reference==
Crystal structures of yeast beta-alanine synthase complexes reveal the mode of substrate binding and large scale domain closure movements., Lundgren S, Andersen B, Piskur J, Dobritzsch D, J Biol Chem. 2007 Dec 7;282(49):36037-47. Epub 2007 Oct 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17916556 17916556]
Crystal structures of yeast beta-alanine synthase complexes reveal the mode of substrate binding and large scale domain closure movements., Lundgren S, Andersen B, Piskur J, Dobritzsch D, J Biol Chem. 2007 Dec 7;282(49):36037-47. Epub 2007 Oct 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17916556 17916556]
 +
 +
Yeast beta-alanine synthase shares a structural scaffold and origin with dizinc-dependent exopeptidases., Lundgren S, Gojkovic Z, Piskur J, Dobritzsch D, J Biol Chem. 2003 Dec 19;278(51):51851-62. Epub 2003 Oct 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14534321 14534321]
 +
 +
Crystallization and preliminary X-ray analysis of beta-alanine synthase from the yeast Saccharomyces kluyveri., Dobritzsch D, Gojkovic Z, Andersen B, Piskur J, Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1267-9. Epub 2003, Jun 27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12832781 12832781]
[[Category: Beta-ureidopropionase]]
[[Category: Beta-ureidopropionase]]
[[Category: Lachancea kluyveri]]
[[Category: Lachancea kluyveri]]
Line 32: Line 40:
[[Category: Di-zinc center]]
[[Category: Di-zinc center]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:22:03 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:53:55 2008''

Revision as of 06:53, 28 July 2008

Image:2v8g.png

Template:STRUCTURE 2v8g

CRYSTAL STRUCTURE OF BETA-ALANINE SYNTHASE FROM SACCHAROMYCES KLUYVERI IN COMPLEX WITH THE PRODUCT BETA-ALANINE

Template:ABSTRACT PUBMED 17916556

About this Structure

2V8G is a Single protein structure of sequence from Lachancea kluyveri. Full crystallographic information is available from OCA.

Reference

Crystal structures of yeast beta-alanine synthase complexes reveal the mode of substrate binding and large scale domain closure movements., Lundgren S, Andersen B, Piskur J, Dobritzsch D, J Biol Chem. 2007 Dec 7;282(49):36037-47. Epub 2007 Oct 4. PMID:17916556

Yeast beta-alanine synthase shares a structural scaffold and origin with dizinc-dependent exopeptidases., Lundgren S, Gojkovic Z, Piskur J, Dobritzsch D, J Biol Chem. 2003 Dec 19;278(51):51851-62. Epub 2003 Oct 8. PMID:14534321

Crystallization and preliminary X-ray analysis of beta-alanine synthase from the yeast Saccharomyces kluyveri., Dobritzsch D, Gojkovic Z, Andersen B, Piskur J, Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1267-9. Epub 2003, Jun 27. PMID:12832781

Page seeded by OCA on Mon Jul 28 09:53:55 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2v8g"
Personal tools