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.


1ah2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ah2.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ah2.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ah2| PDB=1ah2 | SCENE= }}
{{STRUCTURE_1ah2| PDB=1ah2 | SCENE= }}
-
'''SERINE PROTEASE PB92 FROM BACILLUS ALCALOPHILUS, NMR, 18 STRUCTURES'''
+
===SERINE PROTEASE PB92 FROM BACILLUS ALCALOPHILUS, NMR, 18 STRUCTURES===
-
==Overview==
+
<!--
-
BACKGROUND: Research on high-alkaline proteases, such as serine protease PB92, has been largely inspired by their industrial application as protein-degrading components of washing powders. Serine protease PB92 is a member of the subtilase family of enzymes, which has been extensively studied. These studies have included exhaustive protein engineering investigations and X-ray crystallography, in order to provide insight into the mechanism and specificity of enzyme catalysis. Distortions have been observed in the substrate-binding region of subtilisin crystal structures, due to crystal contacts. In addition, the structural variability in the substrate-binding region of subtilisins is often attributed to flexibility. It was hoped that the solution structure of this enzyme would provide further details about the conformation of this key region and give new insights into the functional properties of these enzymes. RESULTS: The three-dimensional solution structure of the 269-residue (27 kDa) serine protease PB92 has been determined using distance and dihedral angle constraints derived from triple-resonance NMR data. The solution structure is represented by a family of 18 conformers which overlay onto the average structure with backbone and all-heavy-atom root mean square deviations (for the main body of the molecule) of 0.88 and 1.21 A, respectively. The family of structures contains a number of regions of relatively high conformational heterogeneity, including various segments that are involved in the formation of the substrate-binding site. The presence of flexibility within these segments has been established from NMR relaxation parameters and measurements of amide proton exchange rates. CONCLUSIONS: The solution structure of the serine protease PB92 presents a well defined global fold which is rigid with the exception of a restricted number of sites. Among the limited number of residues involved in significant internal mobility are those of two pockets, termed S1 and S4, within the substrate-binding site. The presence of flexibility within the binding site supports the proposed induced fit mechanism of substrate binding.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9115441}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9115441 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9115441}}
==About this Structure==
==About this Structure==
-
1AH2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_alcalophilus Bacillus alcalophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AH2 OCA].
+
1AH2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_alcalophilus Bacillus alcalophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AH2 OCA].
==Reference==
==Reference==
Line 33: Line 37:
[[Category: Serine protease]]
[[Category: Serine protease]]
[[Category: Subtilase]]
[[Category: Subtilase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:15:37 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:50:04 2008''

Revision as of 13:50, 30 June 2008

Image:1ah2.png

Template:STRUCTURE 1ah2

SERINE PROTEASE PB92 FROM BACILLUS ALCALOPHILUS, NMR, 18 STRUCTURES

Template:ABSTRACT PUBMED 9115441

About this Structure

1AH2 is a Single protein structure of sequence from Bacillus alcalophilus. Full experimental information is available from OCA.

Reference

The solution structure of serine protease PB92 from Bacillus alcalophilus presents a rigid fold with a flexible substrate-binding site., Martin JR, Mulder FA, Karimi-Nejad Y, van der Zwan J, Mariani M, Schipper D, Boelens R, Structure. 1997 Apr 15;5(4):521-32. PMID:9115441

Page seeded by OCA on Mon Jun 30 16:50:04 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ah2"
Personal tools