1cdg: Difference between revisions
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[[Image:1cdg.gif|left|200px]] | [[Image:1cdg.gif|left|200px]] | ||
'''NUCLEOTIDE SEQUENCE AND X-RAY STRUCTURE OF CYCLODEXTRIN GLYCOSYLTRANSFERASE FROM BACILLUS CIRCULANS STRAIN 251 IN A MALTOSE-DEPENDENT CRYSTAL FORM''' | {{Structure | ||
|PDB= 1cdg |SIZE=350|CAPTION= <scene name='initialview01'>1cdg</scene>, resolution 2.0Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MAL:MALTOSE'>MAL</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Cyclomaltodextrin_glucanotransferase Cyclomaltodextrin glucanotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.19 2.4.1.19] | |||
|GENE= | |||
}} | |||
'''NUCLEOTIDE SEQUENCE AND X-RAY STRUCTURE OF CYCLODEXTRIN GLYCOSYLTRANSFERASE FROM BACILLUS CIRCULANS STRAIN 251 IN A MALTOSE-DEPENDENT CRYSTAL FORM''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1CDG is a [ | 1CDG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_circulans Bacillus circulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CDG OCA]. | ||
==Reference== | ==Reference== | ||
Nucleotide sequence and X-ray structure of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 in a maltose-dependent crystal form., Lawson CL, van Montfort R, Strokopytov B, Rozeboom HJ, Kalk KH, de Vries GE, Penninga D, Dijkhuizen L, Dijkstra BW, J Mol Biol. 1994 Feb 18;236(2):590-600. PMID:[http:// | Nucleotide sequence and X-ray structure of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 in a maltose-dependent crystal form., Lawson CL, van Montfort R, Strokopytov B, Rozeboom HJ, Kalk KH, de Vries GE, Penninga D, Dijkhuizen L, Dijkstra BW, J Mol Biol. 1994 Feb 18;236(2):590-600. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8107143 8107143] | ||
[[Category: Bacillus circulans]] | [[Category: Bacillus circulans]] | ||
[[Category: Cyclomaltodextrin glucanotransferase]] | [[Category: Cyclomaltodextrin glucanotransferase]] | ||
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[[Category: transferase(glucanotransferase)]] | [[Category: transferase(glucanotransferase)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:23:00 2008'' | ||
Revision as of 11:23, 20 March 2008
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| , resolution 2.0Å | |||||||
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| Ligands: | and | ||||||
| Activity: | Cyclomaltodextrin glucanotransferase, with EC number 2.4.1.19 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NUCLEOTIDE SEQUENCE AND X-RAY STRUCTURE OF CYCLODEXTRIN GLYCOSYLTRANSFERASE FROM BACILLUS CIRCULANS STRAIN 251 IN A MALTOSE-DEPENDENT CRYSTAL FORM
OverviewOverview
The cyclodextrin glycosyltransferase (CGTase, EC 2.4.1.19) gene from Bacillus circulans strain 251 was cloned and sequenced. It was found to code for a mature protein of 686 amino acid residues, showing 75% identity to the CGTase from B. circulans strain 8. The X-ray structure of the CGTase was elucidated in a maltodextrin-dependent crystal form and refined against X-ray diffraction data to 2.0 A resolution. The structure of the enzyme is nearly identical to the CGTase from B. circulans strain 8. Three maltose binding sites are observed at the protein surface, two in domain E and one in domain C. The maltose-dependence of CGTase crystallization can be ascribed to the proximity of two of the maltose binding sites to intermolecular crystal contacts. The maltose molecules bound in the E domain interact with several residues implicated in a raw starch binding motif conserved among a diverse group of starch converting enzymes.
About this StructureAbout this Structure
1CDG is a Single protein structure of sequence from Bacillus circulans. Full crystallographic information is available from OCA.
ReferenceReference
Nucleotide sequence and X-ray structure of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 in a maltose-dependent crystal form., Lawson CL, van Montfort R, Strokopytov B, Rozeboom HJ, Kalk KH, de Vries GE, Penninga D, Dijkhuizen L, Dijkstra BW, J Mol Biol. 1994 Feb 18;236(2):590-600. PMID:8107143
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