david lawson (JIC) wrote:
Dear All,
We have solved a structure that has an intersubunit His-His H-bond
(ND1---NE2). The protein most likely undergoes conformational changes
that involve the making and breaking of H-bonds at this interface. In
all the protein structures I have previously studied I don't recall ever
seeing such a bond - His-His ring stacking yes, but never H-bonding. I
was wondering if anyone else had seen this type of interaction and
whether it had any functional significance. The crystals were grown at
pH 5.6.
Many thanks
Dave Lawson
-------------------------------
Dr. David M. Lawson
Biological Chemistry Dept.,
John Innes Centre,
Norwich,
NR4 7UH, UK.
Tel: +44-(0)1603-450725
Fax: +44-(0)1603-450018
Email: [EMAIL PROTECTED]
Web: http://www.jic.bbsrc.ac.uk/staff/david-lawson/index.htm
Dear David,
why not, as long as the histidine residues are not fully protonated, and
at pH 5.6 this is still possible, the nitrogen atoms act as hydrogen
bond donors or acceptors. Look for example in pdb 1FL1 KSHV protease,
where there is a catalytic triad Ser114-His46-His134.
Yours
Wim Burmeister
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Wim Burmeister
Professeur, Membre de l'Institut Universitaire de France
Unit of Virus Host Cell Interactions (UVHCI) UMR5233 UJF-EMBL-CNRS
6 rue Jules Horowitz
B.P. 181, F-38042 Grenoble Cedex 9 FRANCE
E-mail: [EMAIL PROTECTED]
Tel: +33 (0) 476 20 72 82 Fax: +33 (0) 476 20 94 00
http://www2.ujf-grenoble.fr/pharmacie/laboratoires/gdrviro
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