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.


1b90

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1b90.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1b90.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1b90| PDB=1b90 | SCENE= }}
{{STRUCTURE_1b90| PDB=1b90 | SCENE= }}
-
'''BACILLUS CEREUS BETA-AMYLASE APO FORM'''
+
===BACILLUS CEREUS BETA-AMYLASE APO FORM===
-
==Overview==
+
<!--
-
The crystals of beta-amylase from Bacillus cereus belong to space group P21 with the following cell dimensions: a = 57.70 A, b = 92.87 A, c = 65.93 A, and beta =101.95 degrees. The structures of free and maltose-bound beta-amylases were determined by X-ray crystallography at 2.1 and 2.5 A with R-factors of 0.170 and 0.164, respectively. The final model of the maltose-bound form comprises 516 amino acid residues, four maltose molecules, 275 water molecules, one Ca2+, one acetate, and one sulfate ion. The enzyme consists of a core (beta/alpha)8-barrel domain (residues 5-434) and a C-terminal starch-binding domain (residues 435-613). Besides the active site in the core where two maltose molecules are bound in tandem, two novel maltose-binding sites were found in the core L4 region and in the C-terminal domain. The structure of the core domain is similar to that of soybean beta-amylase except for the L4 maltose-binding site, whereas the C-terminal domain has the same secondary structure as domain E of cyclodextrin glucosyltransferase. These two maltose-binding sites are 32-36 A apart from the active site. These results indicate that the ability of B. cereus beta-amylase to digest raw starch can be attributed to the additional two maltose-binding sites.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10353816}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10353816 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10353816}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Shinke, R.]]
[[Category: Shinke, R.]]
[[Category: Utsumi, S.]]
[[Category: Utsumi, S.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:13:32 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:35:52 2008''

Revision as of 15:35, 30 June 2008

Image:1b90.png

Template:STRUCTURE 1b90

BACILLUS CEREUS BETA-AMYLASE APO FORM

Template:ABSTRACT PUBMED 10353816

About this Structure

1B90 is a Single protein structure of sequence from Bacillus cereus. Full crystallographic information is available from OCA.

Reference

Structure of raw starch-digesting Bacillus cereus beta-amylase complexed with maltose., Mikami B, Adachi M, Kage T, Sarikaya E, Nanmori T, Shinke R, Utsumi S, Biochemistry. 1999 Jun 1;38(22):7050-61. PMID:10353816

Page seeded by OCA on Mon Jun 30 18:35:52 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1b90"
Personal tools