This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1h3g

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1h3g.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1h3g.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1h3g| PDB=1h3g | SCENE= }}
{{STRUCTURE_1h3g| PDB=1h3g | SCENE= }}
-
'''CYCLOMALTODEXTRINASE FROM FLAVOBACTERIUM SP. NO. 92: FROM DNA SEQUENCE TO PROTEIN STRUCTURE'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12752453}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12752453 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12752453}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Glycosidase]]
[[Category: Glycosidase]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:23:08 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:34:15 2008''

Revision as of 03:34, 1 July 2008

Image:1h3g.png

Template:STRUCTURE 1h3g

CYCLOMALTODEXTRINASE FROM FLAVOBACTERIUM SP. NO. 92: FROM DNA SEQUENCE TO PROTEIN STRUCTURE

Template:ABSTRACT PUBMED 12752453

About this Structure

1H3G is a Single protein structure of sequence from Flavobacterium sp. 92. 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

Page seeded by OCA on Tue Jul 1 06:34:15 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1h3g"
Personal tools