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.


2yxp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2yxp.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2yxp.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2yxp| PDB=2yxp | SCENE= }}
{{STRUCTURE_2yxp| PDB=2yxp | SCENE= }}
-
'''The Effect of Deuteration on Protein Structure A High Resolution Comparison of Hydrogenous and Perdeuterated Haloalkane Dehalogenase'''
+
===The Effect of Deuteration on Protein Structure A High Resolution Comparison of Hydrogenous and Perdeuterated Haloalkane Dehalogenase===
-
==Overview==
+
<!--
-
Haloalkane dehalogenase from Xanthobacter autotrophicus (XaDHL) was overexpressed under different isotopic conditions to produce fully hydrogenous (h-XaDHL) and perdeuterated (d-XaDHL) enzyme forms. Deuterium atoms at labile positions were allowed to back-exchange during purification and hydrogenous solutions were used for crystallization. Optimal crystals of h-XaDHL and d-XaDHL were obtained under different pH conditions (pH 6.0 and 4.6, respectively) but had similar P2(1)2(1)2 unit cells. X-ray diffraction data were refined to 1.53 A (h-XaDHL) and 1.55 A (d-XaDHL) with excellent overall statistics. The conformations of h-XaDHL and d-XaDHL are similar, with slightly altered surface regions because of different packing environments, and h-XaDHL is found to have a more hydrophobic core than d-XaDHL. The active site of h-XaDHL is similar to those of previously determined structures, but the active site of d-XaDHL unexpectedly has some crucial differences. Asp124, the primary nucleophile in the hydrolysis of haloalkane substrates, is displaced from its position in h-XaDHL and rotates to form a hydrogen bond with His289. As a consequence, the water molecule proposed to function as the nucleophile in the next catalytic step is excluded from the active site. This is the first observation of this unusual active-site configuration, which is obtained as a result of perdeuteration that decreases the hydrophobicity of the enzyme, therefore shifting the optimal pH of crystallization. This d-XaDHL structure is likely to represent the termination state of the catalytic reaction and provides an explanation for the acid inhibition of XaDHL. These results underline the importance of carefully verifying the assumption that isotopic substitution does not produce significant structural changes in protein structures.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17704569}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17704569 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17704569}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Protein deuteration]]
[[Category: Protein deuteration]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 19:39:33 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:03:27 2008''

Revision as of 09:03, 29 July 2008

Image:2yxp.png

Template:STRUCTURE 2yxp

The Effect of Deuteration on Protein Structure A High Resolution Comparison of Hydrogenous and Perdeuterated Haloalkane Dehalogenase

Template:ABSTRACT PUBMED 17704569

About this Structure

2YXP is a Single protein structure of sequence from Xanthobacter autotrophicus. Full crystallographic information is available from OCA.

Reference

The effect of deuteration on protein structure: a high-resolution comparison of hydrogenous and perdeuterated haloalkane dehalogenase., Liu X, Hanson BL, Langan P, Viola RE, Acta Crystallogr D Biol Crystallogr. 2007 Sep;63(Pt 9):1000-8. Epub 2007, Aug 17. PMID:17704569

Page seeded by OCA on Tue Jul 29 12:03:27 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2yxp"
Personal tools