We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1vfk

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1vfk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vfk, resolution 2.90&Aring;" /> '''Crystal structure of...)
Current revision (05:35, 23 September 2009) (edit) (undo)
(Redirecting to 3a6o)
 
(6 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1vfk.gif|left|200px]]<br /><applet load="1vfk" size="450" color="white" frame="true" align="right" spinBox="true"
+
#REDIRECT [[3a6o]] This PDB entry is obsolete and replaced by 3a6o
-
caption="1vfk, resolution 2.90&Aring;" />
+
-
'''Crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase 2/acarbose complex'''<br />
+
-
 
+
-
==Overview==
+
-
Thermoactinomyces vulgaris R-47 alpha-amylase 2 (TVAII) has the unique, ability to hydrolyze cyclodextrins (CDs), with various sized cavities, as, well as starch. To understand the relationship between structure and, substrate specificity, x-ray structures of a TVAII-acarbose complex and, inactive mutant TVAII (D325N/D421N)/alpha-, beta- and gamma-CDs complexes, were determined at resolutions of 2.9, 2.9, 2.8, and 3.1 A, respectively., In all complexes, the interactions between ligands and enzymes at subsites, -1, -2, and -3 were almost the same, but striking differences in the, catalytic site structure were found at subsites +1 and +2, where Trp(356), and Tyr(374) changed the conformation of the side chain depending on the, structure and size of the ligands. Trp(356) and Tyr(374) are thought to be, responsible for the multiple substrate-recognition mechanism of TVAII, providing the unique substrate specificity. In the beta-CD complex, the, beta-CD maintains a regular conical structure, making it difficult for, Glu(354) to protonate the O-4 atom at the hydrolyzing site as a previously, proposed hydrolyzing mechanism of alpha-amylase. From the x-ray, structures, it is suggested that the protonation of the O-4 atom is, possibly carried out via a hydrogen atom of the inter-glucose hydrogen, bond at the hydrolyzing site.
+
-
 
+
-
==About this Structure==
+
-
1VFK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoactinomyces_vulgaris Thermoactinomyces vulgaris] with GLC and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Neopullulanase Neopullulanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.135 3.2.1.135] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VFK OCA].
+
-
 
+
-
==Reference==
+
-
Complex structures of Thermoactinomyces vulgaris R-47 alpha-amylase 2 with acarbose and cyclodextrins demonstrate the multiple substrate recognition mechanism., Ohtaki A, Mizuno M, Tonozuka T, Sakano Y, Kamitori S, J Biol Chem. 2004 Jul 23;279(30):31033-40. Epub 2004 May 11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15138257 15138257]
+
-
[[Category: Neopullulanase]]
+
-
[[Category: Single protein]]
+
-
[[Category: Thermoactinomyces vulgaris]]
+
-
[[Category: Kamitori, S.]]
+
-
[[Category: Mizuno, M.]]
+
-
[[Category: Ohtaki, A.]]
+
-
[[Category: Sakano, Y.]]
+
-
[[Category: Tonozuka, T.]]
+
-
[[Category: CA]]
+
-
[[Category: GLC]]
+
-
[[Category: acarbose]]
+
-
[[Category: amylase]]
+
-
[[Category: complex]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:48:09 2007''
+

Current revision

  1. REDIRECT 3a6o This PDB entry is obsolete and replaced by 3a6o

Proteopedia Page Contributors and Editors (what is this?)

OCA

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