1fmf: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:1fmf.gif|left|200px]]
{{Seed}}
[[Image:1fmf.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1fmf|  PDB=1fmf  |  SCENE=  }}  
{{STRUCTURE_1fmf|  PDB=1fmf  |  SCENE=  }}  


'''REFINED SOLUTION STRUCTURE OF THE (13C,15N-LABELED) B12-BINDING SUBUNIT OF GLUTAMATE MUTASE FROM CLOSTRIDIUM TETANOMORPHUM'''
===REFINED SOLUTION STRUCTURE OF THE (13C,15N-LABELED) B12-BINDING SUBUNIT OF GLUTAMATE MUTASE FROM CLOSTRIDIUM TETANOMORPHUM===




==Overview==
<!--  
Uniformly (13)C,(15)N-labeled MutS, the coenzyme B(12)-binding subunit of glutamate mutase from Clostridium tetanomorphum, was prepared by overexpression from an Escherichia coli strain. Multidimensional heteronuclear NMR spectroscopic experiments with aqueous solutions of (13)C,(15)N-labeled MutS provided signal assignments for roughly 90% of the 1025 hydrogen, 651 carbon, and 173 nitrogen atoms and resulted in about 1800 experimental restraints. Based on the information from the NMR experiments, the structure of MutS was calculated, confirming the earlier, less detailed structure obtained with (15)N-labeled MutS. The refined analysis allowed a precise determination of the secondary and tertiary structure including several crucial side chain interactions. The structures of (the apoprotein) MutS in solution and of the B(12)-binding subunit in the crystal of the corresponding homologous holoenzyme from Clostridium cochlearium differ only in a section that forms the well-structured helix alpha1 in the crystal structure and that also comprises the cobalt-coordinating histidine residue. In the apoprotein MutS, this part of the B(12)-binding subunit is dynamic. The carboxy-terminal end of this section is conformationally flexible and has significant propensity for an alpha-helical structure ("nascent helix"). This dynamic section in MutS is a decisive element for the binding of the nucleotide moiety of coenzyme B(12) and appears to be stabilized as a helix (alpha1) upon trapping of the nucleotide of the B(12) cofactor.
The line below this paragraph, {{ABSTRACT_PUBMED_11828501}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 11828501 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_11828501}}


==About this Structure==
==About this Structure==
1FMF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_tetanomorphum Clostridium tetanomorphum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FMF OCA].  
1FMF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_tetanomorphum Clostridium tetanomorphum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FMF OCA].  


==Reference==
==Reference==
Line 31: Line 35:
[[Category: Nucleotide binding fold]]
[[Category: Nucleotide binding fold]]
[[Category: Rossmann fold]]
[[Category: Rossmann fold]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:30:10 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:29:09 2008''

Revision as of 00:29, 1 July 2008

File:1fmf.png

Template:STRUCTURE 1fmf

REFINED SOLUTION STRUCTURE OF THE (13C,15N-LABELED) B12-BINDING SUBUNIT OF GLUTAMATE MUTASE FROM CLOSTRIDIUM TETANOMORPHUM

Template:ABSTRACT PUBMED 11828501

About this Structure

1FMF is a Single protein structure of sequence from Clostridium tetanomorphum. Full experimental information is available from OCA.

Reference

A protein pre-organized to trap the nucleotide moiety of coenzyme B(12): refined solution structure of the B(12)-binding subunit of glutamate mutase from Clostridium tetanomorphum., Hoffmann B, Tollinger M, Konrat R, Huhta M, Marsh EN, Krautler B, Chembiochem. 2001 Sep 3;2(9):643-55. PMID:11828501

Page seeded by OCA on Tue Jul 1 03:29:09 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1fmf&oldid=597960"