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.


1ys2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ys2.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ys2.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ys2| PDB=1ys2 | SCENE= }}
{{STRUCTURE_1ys2| PDB=1ys2 | SCENE= }}
-
'''Burkholderia cepacia lipase complexed with hexylphosphonic acid (S) 2-methyl-3-phenylpropyl ester'''
+
===Burkholderia cepacia lipase complexed with hexylphosphonic acid (S) 2-methyl-3-phenylpropyl ester===
-
==Overview==
+
<!--
-
Synthetic chemists often exploit the high enantioselectivity of lipases to prepare pure enantiomers of primary alcohols, but the molecular basis for this enantioselectivity is unknown. The crystal structures of two phosphonate transition-state analogs bound to Burkholderia cepacia lipase reveal this molecular basis for a typical primary alcohol: 2-methyl-3-phenyl-1-propanol. The enantiomeric alcohol moieties adopt surprisingly similar orientations, with only subtle differences that make it difficult to predict how to alter enantioselectivity. These structures, along with a survey of previous structures of enzyme bound enantiomers, reveal that binding of enantiomers does not involve an exchange of two substituent positions as most researchers assumed. Instead, the enantiomers adopt mirror-image packing, where three of the four substituents at the stereocenter lie in similar positions. The fourth substituent, hydrogen, points in opposite directions.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15850979}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15850979 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15850979}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Ca2++ ion]]
[[Category: Ca2++ ion]]
[[Category: Cis peptide bond leu 234]]
[[Category: Cis peptide bond leu 234]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:42:45 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:36:22 2008''

Revision as of 02:36, 29 July 2008

Image:1ys2.png

Template:STRUCTURE 1ys2

Burkholderia cepacia lipase complexed with hexylphosphonic acid (S) 2-methyl-3-phenylpropyl ester

Template:ABSTRACT PUBMED 15850979

About this Structure

1YS2 is a Single protein structure of sequence from Burkholderia cepacia. Full crystallographic information is available from OCA.

Reference

Mirror-image packing in enantiomer discrimination molecular basis for the enantioselectivity of B.cepacia lipase toward 2-methyl-3-phenyl-1-propanol., Mezzetti A, Schrag JD, Cheong CS, Kazlauskas RJ, Chem Biol. 2005 Apr;12(4):427-37. PMID:15850979

Page seeded by OCA on Tue Jul 29 05:36:22 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ys2"
Personal tools