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.


2po3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2po3.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2po3.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2po3| PDB=2po3 | SCENE= }}
{{STRUCTURE_2po3| PDB=2po3 | SCENE= }}
-
'''Crystal Structure Analysis of DesI in the presence of its TDP-sugar product'''
+
===Crystal Structure Analysis of DesI in the presence of its TDP-sugar product===
-
==Overview==
+
<!--
-
Desosamine is a 3-(dimethylamino)-3,4,6-trideoxyhexose found, for example, in such macrolide antibiotics as erthyromycin, azithromycin, and clarithromycin. The efficacies of these macrolide antibiotics are markedly reduced in the absence of desosamine. In the bacterium Streptomyces venezuelae, six enzymes are required for the production of dTDP-desosamine. The focus of this X-ray crystallographic analysis is the third enzyme in the pathway, a PLP-dependent aminotransferase referred to as DesI. The structure of DesI was solved in complex with its product, dTDP-4-amino-4,6-dideoxyglucose, to a nominal resolution of 2.1 A. Each subunit of the dimeric enzyme contains 12 alpha-helices and 14 beta-strands. Three cis-peptides are observed in each subunit, Phe 330, Pro 332, and Pro 339. The two active sites of the enzyme are located in clefts at the subunit/subunit interface. Electron density corresponding to the bound product clearly demonstrates a covalent bond between the amino group of the product and C-4' of the PLP cofactor. Interestingly, there are no hydrogen-bonding interactions between the protein and the dideoxyglucosyl group of the product (within 3.2 A). The only other sugar-modifying aminotransferase whose structure is known in the presence of product is PseC from Helicobacter pylori. This enzyme, as opposed to DesI, catalyzes amino transfer to the axial position of the sugar. A superposition of the two active sites for these proteins reveals that the major differences in ligand binding occur in the orientations of the deoxyglucosyl and phosphoryl groups. Indeed, the nearly 180 degrees difference in hexose orientation explains the equatorial versus axial amino transfer exhibited by DesI and PseC, respectively.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17630700}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17630700 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17630700}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Plp]]
[[Category: Plp]]
[[Category: Tdp-sugar]]
[[Category: Tdp-sugar]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 13:31:18 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:49:55 2008''

Revision as of 17:50, 28 July 2008

Image:2po3.png

Template:STRUCTURE 2po3

Crystal Structure Analysis of DesI in the presence of its TDP-sugar product

Template:ABSTRACT PUBMED 17630700

About this Structure

2PO3 is a Single protein structure of sequence from Streptomyces venezuelae. Full crystallographic information is available from OCA.

Reference

Molecular architecture of DesI: a key enzyme in the biosynthesis of desosamine., Burgie ES, Holden HM, Biochemistry. 2007 Aug 7;46(31):8999-9006. Epub 2007 Jul 13. PMID:17630700

Page seeded by OCA on Mon Jul 28 20:49:55 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2po3"
Personal tools