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.

1do2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1do2.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1do2.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1do2| PDB=1do2 | SCENE= }}
{{STRUCTURE_1do2| PDB=1do2 | SCENE= }}
-
'''TRIGONAL CRYSTAL FORM OF HEAT SHOCK LOCUS U (HSLU) FROM ESCHERICHIA COLI'''
+
===TRIGONAL CRYSTAL FORM OF HEAT SHOCK LOCUS U (HSLU) FROM ESCHERICHIA COLI===
-
==Overview==
+
<!--
-
The degradation of cytoplasmic proteins is an ATP-dependent process. Substrates are targeted to a single soluble protease, the 26S proteasome, in eukaryotes and to a number of unrelated proteases in prokaryotes. A surprising link emerged with the discovery of the ATP-dependent protease HslVU (heat shock locus VU) in Escherichia coli. Its protease component HslV shares approximately 20% sequence similarity and a conserved fold with 20S proteasome beta-subunits. HslU is a member of the Hsp100 (Clp) family of ATPases. Here we report the crystal structures of free HslU and an 820,000 relative molecular mass complex of HslU and HslV-the first structure of a complete set of components of an ATP-dependent protease. HslV and HslU display sixfold symmetry, ruling out mechanisms of protease activation that require a symmetry mismatch between the two components. Instead, there is conformational flexibility and domain motion in HslU and a localized order-disorder transition in HslV. Individual subunits of HslU contain two globular domains in relative orientations that correlate with nucleotide bound and unbound states. They are surprisingly similar to their counterparts in N-ethylmaleimide-sensitive fusion protein, the prototype of an AAA-ATPase. A third, mostly alpha-helical domain in HslU mediates the contact with HslV and may be the structural equivalent of the amino-terminal domains in proteasomal AAA-ATPases.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10693812}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10693812 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10693812}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Hslu]]
[[Category: Hslu]]
[[Category: Proteasome]]
[[Category: Proteasome]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:04:10 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:21:28 2008''

Revision as of 20:21, 30 June 2008

Image:1do2.png

Template:STRUCTURE 1do2

TRIGONAL CRYSTAL FORM OF HEAT SHOCK LOCUS U (HSLU) FROM ESCHERICHIA COLI

Template:ABSTRACT PUBMED 10693812

About this Structure

1DO2 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

The structures of HsIU and the ATP-dependent protease HsIU-HsIV., Bochtler M, Hartmann C, Song HK, Bourenkov GP, Bartunik HD, Huber R, Nature. 2000 Feb 17;403(6771):800-5. PMID:10693812

Page seeded by OCA on Mon Jun 30 23:21:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1do2"
Personal tools