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.


1stb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1stb.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1stb.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1stb| PDB=1stb | SCENE= }}
{{STRUCTURE_1stb| PDB=1stb | SCENE= }}
-
'''ACCOMMODATION OF INSERTION MUTATIONS ON THE SURFACE AND IN THE INTERIOR OF STAPHYLOCOCCAL NUCLEASE'''
+
===ACCOMMODATION OF INSERTION MUTATIONS ON THE SURFACE AND IN THE INTERIOR OF STAPHYLOCOCCAL NUCLEASE===
-
==Overview==
+
<!--
-
Alignment of homologous amino acid sequences reveals that insertion mutations are fairly common in evolution. Hitherto, the structural consequences of insertion mutations on the surface and in the interior of proteins of known structures have received little attention. We report here the high-resolution X-ray crystal structures of 2 site-directed insertion mutants of staphylococcal nuclease. The structure of the first insertion mutant, in which 2 glycine residues were inserted on the protein surface in the amino-terminal beta-strand, has been solved to 1.70 A resolution and refined to a crystallographic R value of 0.182. The inserted residues are accommodated in a special 3-residue beta-bulge. A bridging water molecule in the newly created cavity satisfies the hydrogen bonding requirements of the beta-sheet by forming a bifurcated hydrogen bond to 1 beta-strand, and a single hydrogen bond to the other beta-strand. The second insertion mutant contains a single leucine residue inserted at the end of the third beta-strand. The structure was solved to 2.0 A resolution and refined to a final R value of 0.196. The insertion is accommodated in a register shift that changes the conformation of the flexible loop portion of the molecule, relaxing and widening the omega turn. This structural alteration results in changes in position and coordination of a bound calcium ion important for catalysis. These structures illustrate important differences in how amino acid insertions are accommodated: as localized bulges, and as extensive register shifts.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8019410}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8019410 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8019410}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Lattman, E E.]]
[[Category: Lattman, E E.]]
[[Category: Quirk, S.]]
[[Category: Quirk, S.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:06:58 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:28:13 2008''

Revision as of 18:28, 27 July 2008

Image:1stb.png

Template:STRUCTURE 1stb

ACCOMMODATION OF INSERTION MUTATIONS ON THE SURFACE AND IN THE INTERIOR OF STAPHYLOCOCCAL NUCLEASE

Template:ABSTRACT PUBMED 8019410

About this Structure

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

Reference

Accommodation of insertion mutations on the surface and in the interior of staphylococcal nuclease., Keefe LJ, Quirk S, Gittis A, Sondek J, Lattman EE, Protein Sci. 1994 Mar;3(3):391-401. PMID:8019410

Page seeded by OCA on Sun Jul 27 21:28:13 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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