1h3g
From Proteopedia
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| - | [[Image:1h3g. | + | [[Image:1h3g.jpg|left|200px]]<br /><applet load="1h3g" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1h3g" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1h3g, resolution 2.1Å" /> | caption="1h3g, resolution 2.1Å" /> | ||
'''CYCLOMALTODEXTRINASE FROM FLAVOBACTERIUM SP. NO. 92: FROM DNA SEQUENCE TO PROTEIN STRUCTURE'''<br /> | '''CYCLOMALTODEXTRINASE FROM FLAVOBACTERIUM SP. NO. 92: FROM DNA SEQUENCE TO PROTEIN STRUCTURE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1H3G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Flavobacterium_sp._92 Flavobacterium sp. 92] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cyclomaltodextrinase Cyclomaltodextrinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.54 3.2.1.54] | + | 1H3G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Flavobacterium_sp._92 Flavobacterium sp. 92] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cyclomaltodextrinase Cyclomaltodextrinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.54 3.2.1.54] Known structural/functional Site: <scene name='pdbsite=AC1:Ca Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H3G OCA]. |
==Reference== | ==Reference== | ||
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[[Category: signal]] | [[Category: signal]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 15:56:15 2007'' |
Revision as of 13:46, 18 December 2007
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CYCLOMALTODEXTRINASE FROM FLAVOBACTERIUM SP. NO. 92: FROM DNA SEQUENCE TO PROTEIN STRUCTURE
Overview
Starting with oligopeptide sequences and using PCR, the gene of the, cyclodextrinase from Flavobacterium sp. no. 92 was derived from the, genomic DNA. The gene was sequenced and expressed in Escherichia coli; the, gene product was purified and crystallized. An X-ray diffraction analysis, using seleno-methionines with multiwavelength anomalous diffraction, techniques yielded the refined 3D structure at 2.1 A resolution. The, enzyme hydrolyzes alpha(1,4)-glycosidic bonds of cyclodextrins and linear, malto-oligosaccharides. It belongs to the glycosylhydrolase family no. 13, and has a chain fold similar to that of alpha-amylases, cyclodextrin, glycosyltransferases, and other cyclodextrinases. In contrast with most, family members but in agreement with other cyclodextrinases, the enzyme, contains an additional characteristic N-terminal domain of about 100, residues. This domain participates in the formation of a putative, D2-symmetric tetramer but not in cyclodextrin binding at the active center, as observed with the other cyclodextrinases. Moreover, the domain is, located at a position quite different from that of the other, cyclodextrinases. Whether oligomerization facilitates the cyclodextrin, deformation required for hydrolysis is discussed.
About this Structure
1H3G is a Single protein structure of sequence from Flavobacterium sp. 92 with CA as ligand. Active as Cyclomaltodextrinase, with EC number 3.2.1.54 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Covalent and three-dimensional structure of the cyclodextrinase from Flavobacterium sp. no. 92., Fritzsche HB, Schwede T, Schulz GE, Eur J Biochem. 2003 May;270(10):2332-41. PMID:12752453
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