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.


1s5g

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1s5g.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1s5g.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1s5g| PDB=1s5g | SCENE= }}
{{STRUCTURE_1s5g| PDB=1s5g | SCENE= }}
-
'''Structure of Scallop myosin S1 reveals a novel nucleotide conformation'''
+
===Structure of Scallop myosin S1 reveals a novel nucleotide conformation===
-
==Overview==
+
<!--
-
Structural studies of myosin have indicated some of the conformational changes that occur in this protein during the contractile cycle, and we have now observed a conformational change in a bound nucleotide as well. The 3.1-A x-ray structure of the scallop myosin head domain (subfragment 1) in the ADP-bound near-rigor state (lever arm =45 degrees to the helical actin axis) shows the diphosphate moiety positioned on the surface of the nucleotide-binding pocket, rather than deep within it as had been observed previously. This conformation strongly suggests a specific mode of entry and exit of the nucleotide from the nucleotide-binding pocket through the so-called "front door." In addition, using a variety of scallop structures, including a relatively high-resolution 2.75-A nucleotide-free near-rigor structure, we have identified a conserved complex salt bridge connecting the 50-kDa upper and N-terminal subdomains. This salt bridge is present only in crystal structures of muscle myosin isoforms that exhibit a strong reciprocal relationship (also known as coupling) between actin and nucleotide affinity.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15184651}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15184651 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15184651}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Novel conformation of nucleotide]]
[[Category: Novel conformation of nucleotide]]
[[Category: Scallop myosin s1]]
[[Category: Scallop myosin s1]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:19:27 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:46:39 2008''

Revision as of 03:46, 28 July 2008

Template:STRUCTURE 1s5g

Structure of Scallop myosin S1 reveals a novel nucleotide conformation

Template:ABSTRACT PUBMED 15184651

About this Structure

1S5G is a Protein complex structure of sequences from Argopecten irradians. Full crystallographic information is available from OCA.

Reference

Myosin subfragment 1 structures reveal a partially bound nucleotide and a complex salt bridge that helps couple nucleotide and actin binding., Risal D, Gourinath S, Himmel DM, Szent-Gyorgyi AG, Cohen C, Proc Natl Acad Sci U S A. 2004 Jun 15;101(24):8930-5. Epub 2004 Jun 7. PMID:15184651

Page seeded by OCA on Mon Jul 28 06:46:39 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools