1rre: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:
[[Image:1rre.jpg|left|200px]]
{{Seed}}
[[Image:1rre.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1rre|  PDB=1rre  |  SCENE=  }}  
{{STRUCTURE_1rre|  PDB=1rre  |  SCENE=  }}  


'''Crystal structure of E.coli Lon proteolytic domain'''
===Crystal structure of E.coli Lon proteolytic domain===




==Overview==
<!--  
ATP-dependent Lon protease degrades specific short-lived regulatory proteins as well as defective and abnormal proteins in the cell. The crystal structure of the proteolytic domain (P domain) of the Escherichia coli Lon has been solved by single-wavelength anomalous dispersion and refined at 1.75-A resolution. The P domain was obtained by chymotrypsin digestion of the full-length, proteolytically inactive Lon mutant (S679A) or by expression of a recombinant construct encoding only this domain. The P domain has a unique fold and assembles into hexameric rings that likely mimic the oligomerization state of the holoenzyme. The hexamer is dome-shaped, with the six N termini oriented toward the narrower ring surface, which is thus identified as the interface with the ATPase domain in full-length Lon. The catalytic sites lie in a shallow concavity on the wider distal surface of the hexameric ring and are connected to the proximal surface by a narrow axial channel with a diameter of approximately 18 A. Within the active site, the proximity of Lys(722) to the side chain of the mutated Ala(679) and the absence of other potential catalytic side chains establish that Lon employs a Ser(679)-Lys(722) dyad for catalysis. Alignment of the P domain catalytic pocket with those of several Ser-Lys dyad peptide hydrolases provides a model of substrate binding, suggesting that polypeptides are oriented in the Lon active site to allow nucleophilic attack by the serine hydroxyl on the si-face of the peptide bond.
The line below this paragraph, {{ABSTRACT_PUBMED_14665623}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 14665623 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_14665623}}


==About this Structure==
==About this Structure==
Line 36: Line 40:
[[Category: Atp-dependent protease]]
[[Category: Atp-dependent protease]]
[[Category: Catalytic ser-lys dyad]]
[[Category: Catalytic ser-lys dyad]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 07:49:19 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:17:20 2008''

Revision as of 09:17, 28 July 2008

File:1rre.png

Template:STRUCTURE 1rre

Crystal structure of E.coli Lon proteolytic domain

Template:ABSTRACT PUBMED 14665623

About this Structure

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

Reference

The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site., Botos I, Melnikov EE, Cherry S, Tropea JE, Khalatova AG, Rasulova F, Dauter Z, Maurizi MR, Rotanova TV, Wlodawer A, Gustchina A, J Biol Chem. 2004 Feb 27;279(9):8140-8. Epub 2003 Dec 9. PMID:14665623

Page seeded by OCA on Mon Jul 28 12:17:20 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1rre&oldid=698113"