We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2muc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2muc.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2muc.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2muc| PDB=2muc | SCENE= }}
{{STRUCTURE_2muc| PDB=2muc | SCENE= }}
-
'''MUCONATE CYCLOISOMERASE VARIANT F329I'''
+
===MUCONATE CYCLOISOMERASE VARIANT F329I===
-
==Overview==
+
<!--
-
We have refined to 2.3 A resolution two muconate cycloisomerase (MCIase) variant structures, F329I and I54V, that differ from each other and from wild-type in their activity toward cis,cis-muconate (CCM) and substituted CCMs. The working and free R-factors for F329I are 17.4/21.6% and for I54V, 17.6/22.3% with good stereochemistry. Except for the mutated residue, there are no significant changes in structure. To understand the differences in enzymatic properties we docked substituted CCMs and CCM into the active sites of the variants and wild type. The extra space the mutations create appears to account for most of the enzymatic differences. The lack of other structural changes explains why, although structurally equivalent changes occur in chloromuconate cycloisomerase (CMCIase), the changes in themselves do not convert a MCIase into a dehalogenating CMCIase. Reanalysis of the CMCIase structure revealed only one general acid/base, K169. The structural implication is that, in 2-chloro-CCM conversion by CMCIase, the lactone ring of 5-chloromuconolactone rotates before dehalogenation to bring the acidic C4 proton next to K169. Therefore, K169 alone performs both required protonation and deprotonation steps, the first at C5 as in MCIase, and the second, after ring rotation, at C4. This distinguishes CMCIase from alpha/beta barrel isomerases and racemases, which use two different bases.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10336378}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10336378 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10336378}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Substrate specificity]]
[[Category: Substrate specificity]]
[[Category: Variant]]
[[Category: Variant]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:34:57 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:49:29 2008''

Revision as of 12:49, 27 July 2008

Image:2muc.png

Template:STRUCTURE 2muc

MUCONATE CYCLOISOMERASE VARIANT F329I

Template:ABSTRACT PUBMED 10336378

About this Structure

2MUC is a Single protein structure of sequence from Pseudomonas putida. Full crystallographic information is available from OCA.

Reference

Structural basis for the activity of two muconate cycloisomerase variants toward substituted muconates., Schell U, Helin S, Kajander T, Schlomann M, Goldman A, Proteins. 1999 Jan 1;34(1):125-36. PMID:10336378

Page seeded by OCA on Sun Jul 27 15:49:29 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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