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.


2uyo

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2uyo.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2uyo.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2uyo| PDB=2uyo | SCENE= }}
{{STRUCTURE_2uyo| PDB=2uyo | SCENE= }}
-
'''CRYSTAL STRUCTURE OF ML2640C FROM MYCOBACTERIUM LEPRAE IN AN HEXAGONAL CRYSTAL FORM'''
+
===CRYSTAL STRUCTURE OF ML2640C FROM MYCOBACTERIUM LEPRAE IN AN HEXAGONAL CRYSTAL FORM===
-
==Overview==
+
<!--
-
Mycobacterium leprae protein ML2640c belongs to a large family of conserved hypothetical proteins predominantly found in mycobacteria, some of them predicted as putative S-adenosylmethionine (AdoMet)-dependent methyltransferases (MTase). As part of a Structural Genomics initiative on conserved hypothetical proteins in pathogenic mycobacteria, we have determined the structure of ML2640c in two distinct crystal forms. As expected, ML2640c has a typical MTase core domain and binds the methyl donor substrate AdoMet in a manner consistent with other known members of this structural family. The putative acceptor substrate-binding site of ML2640c is a large internal cavity, mostly lined by aromatic and aliphatic side-chain residues, suggesting that a lipid-like molecule might be targeted for catalysis. A flap segment (residues 222-256), which isolates the binding site from the bulk solvent and is highly mobile in the crystal structures, could serve as a gateway to allow substrate entry and product release. The multiple sequence alignment of ML2640c-like proteins revealed that the central alpha/beta core and the AdoMet-binding site are very well conserved within the family. However, the amino acid positions defining the binding site for the acceptor substrate display a higher variability, suggestive of distinct acceptor substrate specificities. The ML2640c crystal structures offer the first structural glimpses at this important family of mycobacterial proteins and lend strong support to their functional assignment as AdoMet-dependent methyltransferases.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17660248}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17660248 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17660248}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Putative methyltransferase]]
[[Category: Putative methyltransferase]]
[[Category: Transferase]]
[[Category: Transferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 17:49:25 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:33:39 2008''

Revision as of 23:33, 27 July 2008

Image:2uyo.png

Template:STRUCTURE 2uyo

CRYSTAL STRUCTURE OF ML2640C FROM MYCOBACTERIUM LEPRAE IN AN HEXAGONAL CRYSTAL FORM

Template:ABSTRACT PUBMED 17660248

About this Structure

2UYO is a Single protein structure of sequence from Mycobacterium leprae. Full crystallographic information is available from OCA.

Reference

The crystal structure of M. leprae ML2640c defines a large family of putative S-adenosylmethionine-dependent methyltransferases in mycobacteria., Grana M, Haouz A, Buschiazzo A, Miras I, Wehenkel A, Bondet V, Shepard W, Schaeffer F, Cole ST, Alzari PM, Protein Sci. 2007 Sep;16(9):1896-904. Epub 2007 Jul 27. PMID:17660248

Page seeded by OCA on Mon Jul 28 02:33:39 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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