1KWH
Structure Analysis AlgQ2, a Macromolecule(alginate)-Binding Periplasmic Protein of Sphingomonas sp. A1.
Summary for 1KWH
Entry DOI | 10.2210/pdb1kwh/pdb |
Descriptor | Macromolecule-Binding Periplasmic Protein, CALCIUM ION (3 entities in total) |
Functional Keywords | binding protein, alginate, protein binding |
Biological source | Sphingomonas sp. |
Total number of polymer chains | 1 |
Total formula weight | 57291.79 |
Authors | Momma, K.,Mikami, B.,Mishima, Y.,Hashimoto, W.,Murata, K. (deposition date: 2002-01-29, release date: 2002-02-13, Last modification date: 2024-03-13) |
Primary citation | Momma, K.,Mikami, B.,Mishima, Y.,Hashimoto, W.,Murata, K. Crystal structure of AlgQ2, a macromolecule (alginate)-binding protein of Sphingomonas sp. A1 at 2.0A resolution. J.Mol.Biol., 316:1051-1059, 2002 Cited by PubMed Abstract: 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. PubMed: 11884143DOI: 10.1006/jmbi.2001.5393 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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