1ji2
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1ji2 |SIZE=350|CAPTION= <scene name='initialview01'>1ji2</scene>, resolution 2.30Å | |PDB= 1ji2 |SIZE=350|CAPTION= <scene name='initialview01'>1ji2</scene>, resolution 2.30Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1bvz|1BVZ]], [[1ji1|1JI1]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ji2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ji2 OCA], [http://www.ebi.ac.uk/pdbsum/1ji2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ji2 RCSB]</span> | ||
}} | }} | ||
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[[Category: Sakano, Y.]] | [[Category: Sakano, Y.]] | ||
[[Category: Tonozuka, T.]] | [[Category: Tonozuka, T.]] | ||
| - | [[Category: CA]] | ||
[[Category: beta/alpha barrel]] | [[Category: beta/alpha barrel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:33:59 2008'' |
Revision as of 18:34, 30 March 2008
| |||||||
| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Neopullulanase, with EC number 3.2.1.135 | ||||||
| Related: | 1BVZ, 1JI1
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Improved X-ray Structure of Thermoactinomyces vulgaris R-47 alpha-Amylase 2
Overview
The X-ray crystal structures of Thermoactinomyces vulgaris R-47 alpha-amylase 1 (TVAI) and alpha-amylase 2 (TVAII) have been determined at 1.6 A and 2.3 A resolution, respectively. The structures of TVAI and TVAII have been refined, R-factor of 0.182 (R(free)=0.206) and 0.179 (0.224), respectively, with good chemical geometries. Both TVAI and TVAII have four domains, N, A, B and C, and all very similar in structure. However, there are some differences in the structures between them. Domain N of TVAI interacts strongly with domains A and B, giving a spherical shape structure to the enzyme, while domain N of TVAII is isolated from the other domains, which leads to the formation of a dimer. TVAI has three bound Ca ions, whereas TVAII has only one. TVAI has eight extra loops compared to TVAII, while TVAII has two extra loops compared to TVAI. TVAI can hydrolyze substrates more efficiently than TVAII with a high molecular mass such as starch, while TVAII is much more active against cyclodextrins than TVAI and other alpha-amylases. A structural comparison of the active sites has clearly revealed this difference in substrate specificity.
About this Structure
1JI2 is a Single protein structure of sequence from Thermoactinomyces vulgaris. Full crystallographic information is available from OCA.
Reference
Crystal structures and structural comparison of Thermoactinomyces vulgaris R-47 alpha-amylase 1 (TVAI) at 1.6 A resolution and alpha-amylase 2 (TVAII) at 2.3 A resolution., Kamitori S, Abe A, Ohtaki A, Kaji A, Tonozuka T, Sakano Y, J Mol Biol. 2002 Apr 26;318(2):443-53. PMID:12051850
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