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.


1orb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1orb.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1orb.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1orb| PDB=1orb | SCENE= }}
{{STRUCTURE_1orb| PDB=1orb | SCENE= }}
-
'''ACTIVE SITE STRUCTURAL FEATURES FOR CHEMICALLY MODIFIED FORMS OF RHODANESE'''
+
===ACTIVE SITE STRUCTURAL FEATURES FOR CHEMICALLY MODIFIED FORMS OF RHODANESE===
-
==Overview==
+
<!--
-
In the course of the reaction catalyzed by rhodanese, the enzyme cycles between two catalytic intermediates, the sulfur-free and the sulfur-substituted (persulfide-containing) forms. The crystal structure of sulfur-free rhodanese, which was prepared in solution and then crystallized, is highly similar to that of sulfur-substituted enzyme. The inactivation of sulfur-free rhodanese with a small molar excess of hydrogen peroxide relies essentially on a modification limited to the active site, consisting of the oxidation of the essential sulfhydryl to sulfenyl group (-S-OH). Upon reaction of the sulfur-free enzyme with monoiodoacetate in the crystal, the Cys-247 side chain with the bound carboxymethyl group is forced into a conformation that allows favorable interactions of the carboxylate with the four peptide NH groups that participate in hydrogen bonding interactions with the transferable sulfur atom of the persulfide group in the sulfur-substituted rhodanese. It is concluded that active site-specific chemical modifications of sulfur-free rhodanese do not lead to significant changes of the protein structure, consistent with a high degree of similarity of the structures of the sulfur-free and sulfur-substituted forms of the enzyme both in solution and in the crystal.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8702871}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8702871 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8702871}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Zanotti, G.]]
[[Category: Zanotti, G.]]
[[Category: Thiosulfate:cyanide sulfurtransferase]]
[[Category: Thiosulfate:cyanide sulfurtransferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:11:08 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:35:13 2008''

Revision as of 15:35, 27 July 2008

Image:1orb.png

Template:STRUCTURE 1orb

ACTIVE SITE STRUCTURAL FEATURES FOR CHEMICALLY MODIFIED FORMS OF RHODANESE

Template:ABSTRACT PUBMED 8702871

About this Structure

1ORB is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Active site structural features for chemically modified forms of rhodanese., Gliubich F, Gazerro M, Zanotti G, Delbono S, Bombieri G, Berni R, J Biol Chem. 1996 Aug 30;271(35):21054-61. PMID:8702871

Page seeded by OCA on Sun Jul 27 18:35:13 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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