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.

1a3v

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1a3v.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1a3v.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1a3v| PDB=1a3v | SCENE= }}
{{STRUCTURE_1a3v| PDB=1a3v | SCENE= }}
-
'''STAPHYLOCOCCAL NUCLEASE, CYCLOPENTANE THIOL DISULFIDE TO V23C VARIANT'''
+
===STAPHYLOCOCCAL NUCLEASE, CYCLOPENTANE THIOL DISULFIDE TO V23C VARIANT===
-
==Overview==
+
<!--
-
We have determined by X-ray crystallography the structures of several variants of staphylococcal nuclease with long flexible straight chain and equivalent length cyclic unnatural amino acid side chains embedded in the protein core. The terminal atoms in the straight side chains are not well defined by the observed electron density even though they remain buried within the protein interior. We have previously observed this behavior and have suggested that it may arise from the addition of side-chain vibrational and oscillational motions with each bond as a side chain grows away from the relatively rigid protein main chain and/or the population of multiple rotamers (Wynn R, Harkins P, Richards FM. Fox RO. 1996. Mobile unnatural amino acid side chains in the core of staphylococcal nuclease. Protein Sci 5:1026-1031). Reduction of the number of degrees of freedom by cyclization of a side chain would be expected to constrain these motions. These side chains are in fact well defined in the structures described here. Over-packing of the protein core results in a 1.0 A shift of helix 1 away from the site of mutation. Additionally, we have determined the structure of a side chain containing a single hydrogen to fluorine atom replacement on a methyl group. A fluorine atom is intermediate in size between methyl group and a hydrogen atom. The fluorine atom is observed in a single position indicating it does not rotate like methyl hydrogen atoms. This change also causes subtle differences in the packing interactions.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9260275}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9260275 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9260275}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Nuclease]]
[[Category: Nuclease]]
[[Category: Unnatural amino acid]]
[[Category: Unnatural amino acid]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:46:22 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:57:19 2008''

Revision as of 12:57, 30 June 2008

Image:1a3v.png

Template:STRUCTURE 1a3v

STAPHYLOCOCCAL NUCLEASE, CYCLOPENTANE THIOL DISULFIDE TO V23C VARIANT

Template:ABSTRACT PUBMED 9260275

About this Structure

1A3V is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

Reference

Comparison of straight chain and cyclic unnatural amino acids embedded in the core of staphylococcal nuclease., Wynn R, Harkins PC, Richards FM, Fox RO, Protein Sci. 1997 Aug;6(8):1621-6. PMID:9260275

Page seeded by OCA on Mon Jun 30 15:57:19 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1a3v"
Personal tools