1z0b

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1z0b.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1z0b.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1z0b| PDB=1z0b | SCENE= }}
{{STRUCTURE_1z0b| PDB=1z0b | SCENE= }}
-
'''Crystal Structure of A. fulgidus Lon proteolytic domain E506A mutant'''
+
===Crystal Structure of A. fulgidus Lon proteolytic domain E506A mutant===
-
==Overview==
+
<!--
-
The atomic-resolution crystal structure of the proteolytic domain (P-domain, residues 415-621) of Archaeoglobus fulgidus B-type Lon protease (wtAfLonB) and the structures of several mutants have revealed significant differences in the conformation of the active-site residues when compared to other known Lon P-domains, despite the conservation of the overall fold. The catalytic Ser509 is facing the solvent and is distant from Lys552, the other member of the catalytic dyad. Instead, the adjacent Asp508 forms an ion pair with the catalytic lysine residue. Glu506, an analog of the putative third catalytic residue from a related Methanococcus jannaschii LonB, also faces the solvent and does not interact with the catalytic dyad. We have established that full-length wtAfLonB is proteolytically active in an ATP-dependent manner. The loss of enzymatic activity of the S509A mutant confirms the functional significance of this residue, while retention of considerable level of activity by the D508A and E506A mutants rules out their critical involvement in catalysis. In contrast to the full-length enzymes, all individually purified P-domains (wild-type and mutants) were inactive, and the mutations had no influence on the active-site structure. These findings raise the possibility that, although isolated proteolytic domains of both AfLonB and E.coli LonA are able to assemble into expected functional hexamers, the presence of the other domains, as well as substrate binding, may be needed to stabilize the productive conformation of their active sites. Thus, the observed conformational variability may reflect the differences in the stability of active-site structures for the proteolytic counterparts of single-chain Lon versus independently folded proteolytic subunits of two-chain AAA+ proteases.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16002085}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16002085 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16002085}}
==About this Structure==
==About this Structure==
Line 20: Line 24:
==Reference==
==Reference==
Atomic-resolution crystal structure of the proteolytic domain of Archaeoglobus fulgidus lon reveals the conformational variability in the active sites of lon proteases., Botos I, Melnikov EE, Cherry S, Kozlov S, Makhovskaya OV, Tropea JE, Gustchina A, Rotanova TV, Wlodawer A, J Mol Biol. 2005 Aug 5;351(1):144-57. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16002085 16002085]
Atomic-resolution crystal structure of the proteolytic domain of Archaeoglobus fulgidus lon reveals the conformational variability in the active sites of lon proteases., Botos I, Melnikov EE, Cherry S, Kozlov S, Makhovskaya OV, Tropea JE, Gustchina A, Rotanova TV, Wlodawer A, J Mol Biol. 2005 Aug 5;351(1):144-57. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16002085 16002085]
 +
 +
Pathological crystallography: case studies of several unusual macromolecular crystals., Dauter Z, Botos I, LaRonde-LeBlanc N, Wlodawer A, Acta Crystallogr D Biol Crystallogr. 2005 Jul;61(Pt 7):967-75. Epub 2005, Jun 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15983420 15983420]
[[Category: Archaeoglobus fulgidus]]
[[Category: Archaeoglobus fulgidus]]
[[Category: Endopeptidase La]]
[[Category: Endopeptidase La]]
Line 35: Line 41:
[[Category: B-type lon]]
[[Category: B-type lon]]
[[Category: Catalytic ser-lys dyad]]
[[Category: Catalytic ser-lys dyad]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:01:49 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:57:12 2008''

Revision as of 10:57, 27 July 2008

Image:1z0b.png

Template:STRUCTURE 1z0b

Crystal Structure of A. fulgidus Lon proteolytic domain E506A mutant

Template:ABSTRACT PUBMED 16002085

About this Structure

1Z0B is a Single protein structure of sequence from Archaeoglobus fulgidus. Full crystallographic information is available from OCA.

Reference

Atomic-resolution crystal structure of the proteolytic domain of Archaeoglobus fulgidus lon reveals the conformational variability in the active sites of lon proteases., Botos I, Melnikov EE, Cherry S, Kozlov S, Makhovskaya OV, Tropea JE, Gustchina A, Rotanova TV, Wlodawer A, J Mol Biol. 2005 Aug 5;351(1):144-57. PMID:16002085

Pathological crystallography: case studies of several unusual macromolecular crystals., Dauter Z, Botos I, LaRonde-LeBlanc N, Wlodawer A, Acta Crystallogr D Biol Crystallogr. 2005 Jul;61(Pt 7):967-75. Epub 2005, Jun 24. PMID:15983420

Page seeded by OCA on Sun Jul 27 13:57:12 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1z0b"
Personal tools