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.

1rcm

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1rcm.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1rcm.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1rcm| PDB=1rcm | SCENE= }}
{{STRUCTURE_1rcm| PDB=1rcm | SCENE= }}
-
'''CRYSTAL STRUCTURE OF A UBIQUITIN-DEPENDENT DEGRADATION SUBSTRATE: A THREE-DISULFIDE FORM OF LYSOZYME'''
+
===CRYSTAL STRUCTURE OF A UBIQUITIN-DEPENDENT DEGRADATION SUBSTRATE: A THREE-DISULFIDE FORM OF LYSOZYME===
-
==Overview==
+
<!--
-
Covalent attachment of ubiquitin marks substrates for proteolysis, but features that identify ubiquitination targets such as chicken egg white lysozyme are poorly understood. Recognition of lysozyme first requires reduction of Cys-6 Cys-127, one of its four native disulfide bonds, and Cys-6,Cys-127-carboxymethylated (6,127-rcm) lysozyme can mimic this three-disulfide intermediate. The 6,127-rcm form of lysozyme is known to retain a substantially native-like conformation in solution, and we demonstrate that it is this folded structure that is recognized for ubiquitination. Because native lysozyme is not a substrate, differences between the native and three-disulfide structures must include features responsible for selective ubiquitination. The 1.9-A resolution crystal structure of 6,127-rcm-lysozyme, reported here, affords a view of this ubiquitin-dependent degradation substrate. Two conformers of 6,127-rcm-lysozyme were obtained in the crystal. These differ uniquely from crystal forms of native lysozyme by displacement of the C-terminal residues. The structures suggest that localized unfolding at the C terminus of three-disulfide lysozyme allows the complex of E3 alpha (ubiquitin-protein ligase) and E2 (ubiquitin-carrier protein) to bind to a surface that includes Lys-1 and the putative ubiquitination site Lys-13. From this we infer that the N-terminal and internal substrate recognition sites on the E3 alpha.E2 complex are separated by approximately 20 A.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8387211}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8387211 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8387211}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Hill, C P.]]
[[Category: Hill, C P.]]
[[Category: Johnston, N L.]]
[[Category: Johnston, N L.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:20:09 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:59:41 2008''

Revision as of 11:59, 27 July 2008

Image:1rcm.png

Template:STRUCTURE 1rcm

CRYSTAL STRUCTURE OF A UBIQUITIN-DEPENDENT DEGRADATION SUBSTRATE: A THREE-DISULFIDE FORM OF LYSOZYME

Template:ABSTRACT PUBMED 8387211

About this Structure

1RCM is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

Reference

Crystal structure of a ubiquitin-dependent degradation substrate: a three-disulfide form of lysozyme., Hill CP, Johnston NL, Cohen RE, Proc Natl Acad Sci U S A. 1993 May 1;90(9):4136-40. PMID:8387211

Page seeded by OCA on Sun Jul 27 14:59:41 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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