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David,
In the structure of uncomplexed monomeric Xenopus dishevelled PDZ domain
(1FOA) with
four members in the asymmetric unit, the hexa-HIS tails of two of the
molecules ( B and D ) are
well ordered and complexed to what we modeled as a cobalt atom ( based
on electron
density and the fact that we had used cobalt-based IMAC chromatography
for purification).
Perhaps in some cases HIS tags can bind cobalt well enough to use its
anomalous signal for MAD or SAD for phasing.
Thomas
Thomas Earnest
Physical Biosciences Division
MS 64R0121
Lawrence Berkeley National Laboratory
Berkeley CA 94720
[EMAIL PROTECTED]
510 486 4603
David Waterman wrote:
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That is interesting. Are these all crystal structures? Does anyone
know of an example where a His-tag is intrinsically ordered in a
crystal structure, and not just because, for example, it is being held
in place by a peptide binding site?
Cheers
David
Bret Church wrote:
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Hi Dan,
As at 2 January 2006 there were 236 structures with at least one
chain containing 5 or more consecutive Histidine residues. Atom
records were used in order to extract out the sequences of the
polypeptides.
Gook luck.
Erdahl Teber
Church Lab
Faculty of Pharmacy
University of Sydney
At 12:44 PM 14/07/2006, you wrote:
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Hello:
I was wondering if anyone knows how many structures there are in pdb
with
poly his-tag coordinates deposited?
Thanks,
Dan
_______________________________________________________
W. Bret Church
Lecturer in Pharmaceutical Chemistry
Faculty of Pharmacy A15
http://www.pharm.usyd.edu.au/ tel: (61-2) 9036-6569
University of Sydney 2006 fax: (61-2) 9351-4391
Australia email: [EMAIL PROTECTED]
http://www.sbio.pharm.usyd.edu.au
or
http://www.churchlab.asn.au
Seminar program for Pharmacy is at
http://www.pharm.usyd.edu.au/news/index.shtml#seminar
Drug Design Amongst the Vines, Hunter Valley,
Australia 3-7 December 2006
http://www.ddconference.com
Sydney Protein Group Website:
http://www.mmb.usyd.edu.au/spg
