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.


2rd8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px <!-- The line below this paragraph, containing "STRUCTURE_2rd8", creates the "Structure Box" on the page. You may change the PDB parameter (which sets the PD...)
Line 1: Line 1:
-
[[Image:2rd8.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2rd8.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2rd8| PDB=2rd8 | SCENE= }}
{{STRUCTURE_2rd8| PDB=2rd8 | SCENE= }}
-
'''Human Thymidylate Synthase Stabilized in Active Conformation by R163K Mutation: Asymmetry and Reactivity of Cys195'''
+
===Human Thymidylate Synthase Stabilized in Active Conformation by R163K Mutation: Asymmetry and Reactivity of Cys195===
-
==Overview==
+
<!--
-
Loop 181-197 of human thymidylate synthase (hTS) populates two conformational states. In the first state, Cys195, a residue crucial for catalytic activity, is in the active site (active conformer); in the other conformation, it is about 10 A away, outside the active site (inactive conformer). We have designed and expressed an hTS variant, R163K, in which the inactive conformation is destabilized. The activity of this mutant is 33% higher than that of wt hTS, suggesting that at least one-third of hTS populates the inactive conformer. Crystal structures of R163K in two different crystal forms, with six and two subunits per asymmetric part of the unit cells, have been determined. All subunits of this mutant are in the active conformation while wt hTS crystallizes as the inactive conformer in similar mother liquors. The structures show differences in the environment of catalytic Cys195, which correlate with Cys195 thiol reactivity, as judged by its oxidation state. Calculations show that the molecular electrostatic potential at Cys195 differs between the subunits of the dimer. One of the dimers is asymmetric with a phosphate ion bound in only one of the subunits. In the absence of the phosphate ion, that is in the inhibitor-free enzyme, the tip of loop 47-53 is about 11 A away from the active site.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18370400}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18370400 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18370400}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Methyltransferase]]
[[Category: Methyltransferase]]
[[Category: Nucleotide biosynthesis]]
[[Category: Nucleotide biosynthesis]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 28 09:14:46 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:03:50 2008''

Revision as of 10:03, 28 July 2008

Image:2rd8.png

Template:STRUCTURE 2rd8

Human Thymidylate Synthase Stabilized in Active Conformation by R163K Mutation: Asymmetry and Reactivity of Cys195

Template:ABSTRACT PUBMED 18370400

About this Structure

2RD8 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The R163K mutant of human thymidylate synthase is stabilized in an active conformation: structural asymmetry and reactivity of cysteine 195., Gibson LM, Lovelace LL, Lebioda L, Biochemistry. 2008 Apr 22;47(16):4636-43. Epub 2008 Mar 28. PMID:18370400

Page seeded by OCA on Mon Jul 28 13:03:50 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2rd8"
Personal tools