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.

1jd7

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1jd7.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1jd7.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1jd7| PDB=1jd7 | SCENE= }}
{{STRUCTURE_1jd7| PDB=1jd7 | SCENE= }}
-
'''CRYSTAL STRUCTURE ANALYSIS OF THE MUTANT K300R OF PSEUDOALTEROMONAS HALOPLANCTIS ALPHA-AMYLASE'''
+
===CRYSTAL STRUCTURE ANALYSIS OF THE MUTANT K300R OF PSEUDOALTEROMONAS HALOPLANCTIS ALPHA-AMYLASE===
-
==Overview==
+
<!--
-
To further investigate the mechanism and function of allosteric activation by chloride in some alpha-amylases, the structure of the bacterial alpha-amylase from the psychrophilic micro-organism Pseudoalteromonas haloplanktis in complex with nitrate has been solved at 2.1 A degrees, as well as the structure of the mutants Lys300Gln (2.5 A degrees ) and Lys300Arg (2.25 A degrees ). Nitrate binds strongly to alpha-amylase but is a weak activator. Mutation of the critical chloride ligand Lys300 into Gln results in a chloride-independent enzyme, whereas the mutation into Arg mimics the binding site as is found in animal alpha-amylases with, however, a lower affinity for chloride. These structures reveal that the triangular conformation of the chloride ligands and the nearly equatorial coordination allow the perfect accommodation of planar trigonal monovalent anions such as NO3-, explaining their unusual strong binding. It is also shown that a localized negative charge such as that of Cl-, rather than a delocalized charge as in the case of nitrate, is essential for maximal activation. The chloride-free mutant Lys300Gln indicates that chloride is not mandatory for the catalytic mechanism but strongly increases the reactivity at the active site. Disappearance of the putative catalytic water molecule in this weakly active mutant supports the view that chloride helps to polarize the hydrolytic water molecule and enhances the rate of the second step in the catalytic reaction.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12021442}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12021442 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12021442}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Alpha-beta barrel]]
[[Category: Alpha-beta barrel]]
[[Category: Glycosyl hydrolase]]
[[Category: Glycosyl hydrolase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:04:51 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:03:33 2008''

Revision as of 17:03, 1 July 2008

Image:1jd7.png

Template:STRUCTURE 1jd7

CRYSTAL STRUCTURE ANALYSIS OF THE MUTANT K300R OF PSEUDOALTEROMONAS HALOPLANCTIS ALPHA-AMYLASE

Template:ABSTRACT PUBMED 12021442

About this Structure

1JD7 is a Single protein structure of sequence from Pseudoalteromonas haloplanktis. Full crystallographic information is available from OCA.

Reference

Structural basis of alpha-amylase activation by chloride., Aghajari N, Feller G, Gerday C, Haser R, Protein Sci. 2002 Jun;11(6):1435-41. PMID:12021442

Page seeded by OCA on Tue Jul 1 20:03:33 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1jd7"
Personal tools