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.


1nc1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1nc1.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1nc1.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1nc1| PDB=1nc1 | SCENE= }}
{{STRUCTURE_1nc1| PDB=1nc1 | SCENE= }}
-
'''Crystal structure of E. coli MTA/AdoHcy nucleosidase complexed with 5'-methylthiotubercidin (MTH)'''
+
===Crystal structure of E. coli MTA/AdoHcy nucleosidase complexed with 5'-methylthiotubercidin (MTH)===
-
==Overview==
+
<!--
-
5'-Methylthioadenosine/S-adenosylhomocysteine (MTA/AdoHcy) nucleosidase is a key enzyme in a number of critical biological processes in many microbes. This nucleosidase catalyzes the irreversible hydrolysis of the N(9)-C(1') bond of MTA or AdoHcy to form adenine and the corresponding thioribose. The key role of the MTA/AdoHcy nucleosidase in biological methylation, polyamine biosynthesis, methionine recycling, and bacterial quorum sensing has made it an important antimicrobial drug target. The crystal structures of Escherichia coli MTA/AdoHcy nucleosidase complexed with the transition state analog, formycin A (FMA), and the nonhydrolyzable substrate analog, 5'-methylthiotubercidin (MTT) have been solved to 2.2- and 2.0-A resolution, respectively. These are the first MTA/AdoHcy nucleosidase structures to be solved in the presence of inhibitors. These structures clearly identify the residues involved in substrate binding and catalysis in the active site. Comparisons of the inhibitor complexes to the adenine-bound MTA/AdoHcy nucleosidase (Lee, J. E., Cornell, K. A., Riscoe, M. K., and Howell, P. L. (2001) Structure (Camb.) 9, 941-953) structure provide evidence for a ligand-induced conformational change in the active site and the substrate preference of the enzyme. The enzymatic mechanism has been re-examined.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12496243}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12496243 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12496243}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Riscoe, M K.]]
[[Category: Riscoe, M K.]]
[[Category: Mixed alpha/beta dimer]]
[[Category: Mixed alpha/beta dimer]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:21:07 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:32:39 2008''

Revision as of 08:32, 28 July 2008

Image:1nc1.png

Template:STRUCTURE 1nc1

Crystal structure of E. coli MTA/AdoHcy nucleosidase complexed with 5'-methylthiotubercidin (MTH)

Template:ABSTRACT PUBMED 12496243

About this Structure

1NC1 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure of Escherichia coli 5'-methylthioadenosine/ S-adenosylhomocysteine nucleosidase inhibitor complexes provide insight into the conformational changes required for substrate binding and catalysis., Lee JE, Cornell KA, Riscoe MK, Howell PL, J Biol Chem. 2003 Mar 7;278(10):8761-70. Epub 2002 Dec 20. PMID:12496243

Page seeded by OCA on Mon Jul 28 11:32:39 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1nc1"
Personal tools