1kwh

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(New page: 200px<br /><applet load="1kwh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kwh, resolution 2.00&Aring;" /> '''Structure Analysis A...)
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caption="1kwh, resolution 2.00&Aring;" />
'''Structure Analysis AlgQ2, a Macromolecule(alginate)-Binding Periplasmic Protein of Sphingomonas sp. A1.'''<br />
'''Structure Analysis AlgQ2, a Macromolecule(alginate)-Binding Periplasmic Protein of Sphingomonas sp. A1.'''<br />
==Overview==
==Overview==
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Sphingomonas sp. A1 possesses a high molecular mass (average 25,700 Da), alginate uptake system mediated by a novel pit-dependent ABC transporter., The X-ray crystallographic structure of AlgQ2 (57,200 Da), an, alginate-binding protein in the system, was determined by the multiple, isomorphous replacement method and refined at 2.0 A resolution with a, final R-factor of 18.3% for 15 to 2.0 A resolution data. The refined, structure of AlgQ2 was comprised of 492 amino acid residues, 172 water, molecules, and one calcium ion. AlgQ2 was composed of two globular domains, with a deep cleft between them, which is expected to be the, alginate-binding site. The overall structure is basically similar to that, of maltose/maltodextrin-binding protein, except for the presence of an, N2-subdomain. The entire calcium ion-binding site is similar to the site, in the EF-hand motif, but comprises a ten residue loop. This calcium, ion-binding site is about 40 A away from the alginate-binding site.
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Sphingomonas sp. A1 possesses a high molecular mass (average 25,700 Da) alginate uptake system mediated by a novel pit-dependent ABC transporter. The X-ray crystallographic structure of AlgQ2 (57,200 Da), an alginate-binding protein in the system, was determined by the multiple isomorphous replacement method and refined at 2.0 A resolution with a final R-factor of 18.3% for 15 to 2.0 A resolution data. The refined structure of AlgQ2 was comprised of 492 amino acid residues, 172 water molecules, and one calcium ion. AlgQ2 was composed of two globular domains with a deep cleft between them, which is expected to be the alginate-binding site. The overall structure is basically similar to that of maltose/maltodextrin-binding protein, except for the presence of an N2-subdomain. The entire calcium ion-binding site is similar to the site in the EF-hand motif, but comprises a ten residue loop. This calcium ion-binding site is about 40 A away from the alginate-binding site.
==About this Structure==
==About this Structure==
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1KWH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sphingomonas_sp. Sphingomonas sp.] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KWH OCA].
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1KWH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sphingomonas_sp. Sphingomonas sp.] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KWH OCA].
==Reference==
==Reference==
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[[Category: binding protein]]
[[Category: binding protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:04:51 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:38:42 2008''

Revision as of 11:38, 21 February 2008


1kwh, resolution 2.00Å

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Structure Analysis AlgQ2, a Macromolecule(alginate)-Binding Periplasmic Protein of Sphingomonas sp. A1.

Overview

Sphingomonas sp. A1 possesses a high molecular mass (average 25,700 Da) alginate uptake system mediated by a novel pit-dependent ABC transporter. The X-ray crystallographic structure of AlgQ2 (57,200 Da), an alginate-binding protein in the system, was determined by the multiple isomorphous replacement method and refined at 2.0 A resolution with a final R-factor of 18.3% for 15 to 2.0 A resolution data. The refined structure of AlgQ2 was comprised of 492 amino acid residues, 172 water molecules, and one calcium ion. AlgQ2 was composed of two globular domains with a deep cleft between them, which is expected to be the alginate-binding site. The overall structure is basically similar to that of maltose/maltodextrin-binding protein, except for the presence of an N2-subdomain. The entire calcium ion-binding site is similar to the site in the EF-hand motif, but comprises a ten residue loop. This calcium ion-binding site is about 40 A away from the alginate-binding site.

About this Structure

1KWH is a Single protein structure of sequence from Sphingomonas sp. with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of AlgQ2, a macromolecule (alginate)-binding protein of Sphingomonas sp. A1 at 2.0A resolution., Momma K, Mikami B, Mishima Y, Hashimoto W, Murata K, J Mol Biol. 2002 Mar 8;316(5):1051-9. PMID:11884143

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