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.


2ohy

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2ohy.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2ohy.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2ohy| PDB=2ohy | SCENE= }}
{{STRUCTURE_2ohy| PDB=2ohy | SCENE= }}
-
'''X-ray Crystal Structure of Tyrosine Aminomutase from streptomyces globisporus'''
+
===X-ray Crystal Structure of Tyrosine Aminomutase from streptomyces globisporus===
-
==Overview==
+
<!--
-
The SgcC4 l-tyrosine 2,3-aminomutase (SgTAM) catalyzes the formation of (S)-beta-tyrosine in the biosynthetic pathway of the enediyne antitumor antibiotic C-1027. SgTAM is homologous to the histidine ammonia lyase family of enzymes whose activity is dependent on the methylideneimidazole-5-one (MIO) cofactor. Unlike the lyase enzymes, SgTAM catalyzes additional chemical transformations resulting in an overall stereospecific 1,2-amino shift in the substrate l-tyrosine to generate (S)-beta-tyrosine. Previously, we provided kinetic, spectroscopic, and mutagenesis data supporting the presence of MIO in the active site of SgTAM [Christenson, S. D.; Wu, W.; Spies, A.; Shen, B.; and Toney, M. D. (2003) Biochemistry 42, 12708-12718]. Here we report the first X-ray crystal structure of an MIO-containing aminomutase, SgTAM, and confirm the structural homology of SgTAM to ammonia lyases. Comparison of the structure of SgTAM to the l-tyrosine ammonia lyase from Rhodobacter sphaeroides provides insight into the structural basis for aminomutase activity. The results show that SgTAM has a closed active site well suited to retain ammonia and minimize the formation of lyase elimination products. The amino acid determinants for substrate recognition and catalysis can be predicted from the structure, setting the framework for detailed mechanistic investigations.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17516659}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17516659 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17516659}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: 4-methylideneimidizole-5-one]]
[[Category: 4-methylideneimidizole-5-one]]
[[Category: Mio]]
[[Category: Mio]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:57:48 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:08:16 2008''

Revision as of 04:08, 28 July 2008

Image:2ohy.png

Template:STRUCTURE 2ohy

X-ray Crystal Structure of Tyrosine Aminomutase from streptomyces globisporus

Template:ABSTRACT PUBMED 17516659

About this Structure

2OHY is a Single protein structure of sequence from Streptomyces globisporus. Full crystallographic information is available from OCA.

Reference

The structure of L-tyrosine 2,3-aminomutase from the C-1027 enediyne antitumor antibiotic biosynthetic pathway., Christianson CV, Montavon TJ, Van Lanen SG, Shen B, Bruner SD, Biochemistry. 2007 Jun 19;46(24):7205-14. Epub 2007 May 22. PMID:17516659

Page seeded by OCA on Mon Jul 28 07:08:16 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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