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.


5abp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:5abp.gif|left|200px]]
+
{{Seed}}
 +
[[Image:5abp.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_5abp| PDB=5abp | SCENE= }}
{{STRUCTURE_5abp| PDB=5abp | SCENE= }}
-
'''SUBSTRATE SPECIFICITY AND AFFINITY OF A PROTEIN MODULATED BY BOUND WATER MOLECULES'''
+
===SUBSTRATE SPECIFICITY AND AFFINITY OF A PROTEIN MODULATED BY BOUND WATER MOLECULES===
-
==Overview==
+
<!--
-
Water molecules influence molecular interactions in all biological systems, yet it is extremely difficult to understand their effects in precise atomic detail. Here we present evidence, based on highly refined atomic structures of the complexes of the L-arabinose-binding protein with L-arabinose, D-fucose and D-galactose, that bound water molecules, coupled with localized conformational changes, can govern substrate specificity and affinity. The atoms common to the three sugars are identically positioned in the binding site and the same nine strong hydrogen bonds are formed in all three complexes. Two hydrogen-bonded water molecules in the site contribute further to tight binding of L-arabinose but create an unfavourable interaction with the methyl group of D-fucose. Equally tight binding of D-galactose is attained by the replacement of one of the hydrogen-bonded water molecules by its--CH2OH group, coordinated with localized structural changes which include a shift and redirection of the hydrogen-bonding interactions of the other water molecule. These observations illustrate how ordered water molecules can contribute directly to the properties of proteins by influencing their interaction with ligands.
+
The line below this paragraph, {{ABSTRACT_PUBMED_2818726}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 2818726 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_2818726}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Wilson, D K.]]
[[Category: Wilson, D K.]]
[[Category: Binding protein]]
[[Category: Binding protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:31:40 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:55:35 2008''

Revision as of 10:55, 3 July 2008

Image:5abp.png

Template:STRUCTURE 5abp

SUBSTRATE SPECIFICITY AND AFFINITY OF A PROTEIN MODULATED BY BOUND WATER MOLECULES

Template:ABSTRACT PUBMED 2818726

About this Structure

5ABP is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Substrate specificity and affinity of a protein modulated by bound water molecules., Quiocho FA, Wilson DK, Vyas NK, Nature. 1989 Aug 3;340(6232):404-7. PMID:2818726

Page seeded by OCA on Thu Jul 3 13:55:35 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5abp"
Personal tools