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.

1lvk

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1lvk.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1lvk.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1lvk| PDB=1lvk | SCENE= }}
{{STRUCTURE_1lvk| PDB=1lvk | SCENE= }}
-
'''X-RAY CRYSTAL STRUCTURE OF THE MG (DOT) 2'(3')-O-(N-METHYLANTHRANILOYL) NUCLEOTIDE BOUND TO DICTYOSTELIUM DISCOIDEUM MYOSIN MOTOR DOMAIN'''
+
===X-RAY CRYSTAL STRUCTURE OF THE MG (DOT) 2'(3')-O-(N-METHYLANTHRANILOYL) NUCLEOTIDE BOUND TO DICTYOSTELIUM DISCOIDEUM MYOSIN MOTOR DOMAIN===
-
==Overview==
+
<!--
-
Mant (2'(3')-O-(N-methylanthraniloyl)) labeled nucleotides have proven to be useful tools in the study of the kinetic mechanism of the myosin ATPase by fluorescence spectroscopy. The sensitivity of the mant fluorophore to its local environment also makes it suitable to investigate the exposure of bound nucleotides to solvent from collisional quenching measurements. Here we present the crystal structure of mant-ADP and beryllium fluoride complexed with Dictyostelium discoideum myosin motor domain (S1dC) at 1.9 A resolution. We complement the structural approach with an investigation of the accessibility of the mant moiety to solvent using acrylamide quenching of fluorescence emission. In contrast to rabbit skeletal myosin subfragment 1, where the mant group is protected from acrylamide (Ksv=0.2 M-1), the fluorophore is relatively exposed when bound to Dictyostelium myosin motor domain (Ksv= 1.4 M-1). Differences between the Dictyostelium structure and that of vertebrate skeletal subfragment 1, in the region of the nucleotide binding pocket, are proposed as an explanation for the differences observed in the solvent accessibility of complexed mant-nucleotides. We conclude that protection of the mant group from acrylamide quenching does not report on overall closure of the nucleotide binding pocket but reflects more local structural changes.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9405148}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9405148 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9405148}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Motor]]
[[Category: Motor]]
[[Category: Myosin]]
[[Category: Myosin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:20:19 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 22:27:32 2008''

Revision as of 19:27, 2 July 2008

Image:1lvk.png

Template:STRUCTURE 1lvk

X-RAY CRYSTAL STRUCTURE OF THE MG (DOT) 2'(3')-O-(N-METHYLANTHRANILOYL) NUCLEOTIDE BOUND TO DICTYOSTELIUM DISCOIDEUM MYOSIN MOTOR DOMAIN

Template:ABSTRACT PUBMED 9405148

About this Structure

1LVK is a Single protein structure of sequence from Dictyostelium discoideum. Full crystallographic information is available from OCA.

Reference

X-ray crystal structure and solution fluorescence characterization of Mg.2'(3')-O-(N-methylanthraniloyl) nucleotides bound to the Dictyostelium discoideum myosin motor domain., Bauer CB, Kuhlman PA, Bagshaw CR, Rayment I, J Mol Biol. 1997 Dec 5;274(3):394-407. PMID:9405148

Page seeded by OCA on Wed Jul 2 22:27:32 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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