1gyk

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==Overview==
==Overview==
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Two monoclinic (P2(1)) crystal forms of human serum amyloid P component, (SAP) in complex with the 4,6-pyruvate acetal of beta-D-galactose, (MObetaDG) were prepared. Structure analysis by molecular replacement and, refinement at 2.2A resolution revealed that crystal form 1 (a=95.76A, b=70.53A, c=103.41A, beta=96.80 degrees) 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 2.6A resolution structure of crystal form 2, (a=118.60A, b=109.10A, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?12126626 (full description)]]
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Two monoclinic (P2(1)) crystal forms of human serum amyloid P component, (SAP) in complex with the 4,6-pyruvate acetal of beta-D-galactose, (MObetaDG) were prepared. Structure analysis by molecular replacement and, refinement at 2.2A resolution revealed that crystal form 1 (a=95.76A, b=70.53A, c=103.41A, beta=96.80 degrees) 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 2.6A resolution structure of crystal form 2, (a=118.60A, b=109.10A, c=120.80A and beta=95.16 degrees ) 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 MObetaDG at the interface.
==About this Structure==
==About this Structure==
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1GYK is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with CA and CDG as [[http://en.wikipedia.org/wiki/ligands ligands]]. Structure known Active Site: CA1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GYK OCA]].
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1GYK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA and CDG as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: CA1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GYK OCA].
==Reference==
==Reference==
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[[Category: polymorphism]]
[[Category: polymorphism]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:22:57 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:38:48 2007''

Revision as of 11:33, 5 November 2007


1gyk, resolution 2.2Å

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SERUM AMYLOID P COMPONENT CO-CRYSTALLISED WITH MOBDG AT NEUTRAL PH

Overview

Two monoclinic (P2(1)) crystal forms of human serum amyloid P component, (SAP) in complex with the 4,6-pyruvate acetal of beta-D-galactose, (MObetaDG) were prepared. Structure analysis by molecular replacement and, refinement at 2.2A resolution revealed that crystal form 1 (a=95.76A, b=70.53A, c=103.41A, beta=96.80 degrees) 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 2.6A resolution structure of crystal form 2, (a=118.60A, b=109.10A, c=120.80A and beta=95.16 degrees ) 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 MObetaDG at the interface.

About this Structure

1GYK is a Single protein structure of sequence from Homo sapiens with CA and CDG as ligands. Structure known Active Site: CA1. Full crystallographic information is available from OCA.

Reference

The structures of crystalline complexes of human serum amyloid P component with its carbohydrate ligand, the cyclic pyruvate acetal of galactose., Thompson D, Pepys MB, Tickle I, Wood S, J Mol Biol. 2002 Jul 26;320(5):1081-6. PMID:12126626

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