The Structures of Crystalline Complexes of Human
Serum Amyloid P Component with Its Carbohydrate
Ligand, The Cyclic Pyruvate Acetal of Galactose
The Structures of Crystalline Complexes of Human
Serum Amyloid P Component with Its Carbohydrate
Ligand, The Cyclic Pyruvate Acetal of Galactose
Two monoclinic (P21) crystal forms of human serum amyloid P component
(SAP) in complex with the 4,6-pyruvate acetal of b-D-galactose
(MObDG) were prepared. Structure analysis by molecular replacement
and refinement at 2.2 A ° resolution revealed that crystal form 1
(a 1/4 95:76 A; b 1/4 70:53 A; c 1/4 103:41 A; b 1/4 96:808) contained a pentamer
in the asymmetric unit with a structure very similar to that of the published
search model. The mode of ligand co-ordination was also similar
except that four of the five subunits showed bound ligand with an
additional H-bond between O1 of the galactose and the side-chain of
Lys79. One sub-unit showed no bound ligand and a vacant calcium site
close to a crystal contact. The 2.6 A ° resolution structure of crystal form 2
(a 1/4 118:60 A; b 1/4 109:10 A; c 1/4 120:80 A and b 1/4 95:168) showed ten
sub-units in the asymmetric unit, all with two bound calcium ions and
ligand. The most extensive protein–protein interactions between pentamers
describe an AB face-to-face interaction involving 15 ion pairs that
sandwiches five molecules of bound MObDG at the interface.
1081-1086
Thompson, D.
f02914bc-43d6-4944-91f6-6ee85e697788
Pepys, M.B.
eb147030-b7f9-448a-9d69-9adb72fe7ed2
Tickle, I.
e3c9b336-70b4-498a-acb5-fddd2216fc1d
Wood, S.
c6b0bfe1-a0bc-4e57-84dd-60a8f936dae8
26 July 2002
Thompson, D.
f02914bc-43d6-4944-91f6-6ee85e697788
Pepys, M.B.
eb147030-b7f9-448a-9d69-9adb72fe7ed2
Tickle, I.
e3c9b336-70b4-498a-acb5-fddd2216fc1d
Wood, S.
c6b0bfe1-a0bc-4e57-84dd-60a8f936dae8
Thompson, D., Pepys, M.B., Tickle, I. and Wood, S.
(2002)
The Structures of Crystalline Complexes of Human
Serum Amyloid P Component with Its Carbohydrate
Ligand, The Cyclic Pyruvate Acetal of Galactose.
Journal of Molecular Biology, 320 (5), .
(doi:10.1016/S0022-2836(02)00514-4).
Abstract
Two monoclinic (P21) crystal forms of human serum amyloid P component
(SAP) in complex with the 4,6-pyruvate acetal of b-D-galactose
(MObDG) were prepared. Structure analysis by molecular replacement
and refinement at 2.2 A ° resolution revealed that crystal form 1
(a 1/4 95:76 A; b 1/4 70:53 A; c 1/4 103:41 A; b 1/4 96:808) contained a pentamer
in the asymmetric unit with a structure very similar to that of the published
search model. The mode of ligand co-ordination was also similar
except that four of the five subunits showed bound ligand with an
additional H-bond between O1 of the galactose and the side-chain of
Lys79. One sub-unit showed no bound ligand and a vacant calcium site
close to a crystal contact. The 2.6 A ° resolution structure of crystal form 2
(a 1/4 118:60 A; b 1/4 109:10 A; c 1/4 120:80 A and b 1/4 95:168) showed ten
sub-units in the asymmetric unit, all with two bound calcium ions and
ligand. The most extensive protein–protein interactions between pentamers
describe an AB face-to-face interaction involving 15 ion pairs that
sandwiches five molecules of bound MObDG at the interface.
Text
sap_mob.(4)pdf.pdf
- Other
Restricted to Registered users only
More information
Submitted date: 25 January 2002
Published date: 26 July 2002
Identifiers
Local EPrints ID: 35625
URI: http://eprints.soton.ac.uk/id/eprint/35625
ISSN: 0022-2836
PURE UUID: 28a34fc3-2c9b-4e48-9cf6-6d763c62d853
Catalogue record
Date deposited: 22 May 2006
Last modified: 15 Mar 2024 07:53
Export record
Altmetrics
Contributors
Author:
D. Thompson
Author:
M.B. Pepys
Author:
I. Tickle
Author:
S. Wood
Download statistics
Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.
View more statistics