1bag: Difference between revisions

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New page: left|200px<br /> <applet load="1bag" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bag, resolution 2.5Å" /> '''ALPHA-AMYLASE FROM B...
 
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==About this Structure==
==About this Structure==
1BAG is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]] with CA as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BAG OCA]].  
1BAG is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]] with CA as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1]]. Structure known Active Sites: CA1, CA2 and CA3. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BAG OCA]].  


==Reference==
==Reference==
Crystal structure of a catalytic-site mutant alpha-amylase from Bacillus subtilis complexed with maltopentaose., Fujimoto Z, Takase K, Doui N, Momma M, Matsumoto T, Mizuno H, J Mol Biol. 1998 Mar 27;277(2):393-407. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9514750 9514750]
Crystal structure of a catalytic-site mutant alpha-amylase from Bacillus subtilis complexed with maltopentaose., Fujimoto Z, Takase K, Doui N, Momma M, Matsumoto T, Mizuno H, J Mol Biol. 1998 Mar 27;277(2):393-407. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9514750 9514750]
[[Category: Alpha-amylase]]
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: maltopentaose]]
[[Category: maltopentaose]]


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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:04:45 2007''

Revision as of 14:00, 30 October 2007

File:1bag.gif


1bag, resolution 2.5Å

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ALPHA-AMYLASE FROM BACILLUS SUBTILIS COMPLEXED WITH MALTOPENTAOSE

OverviewOverview

The X-ray crystal structure of a catalytic-site mutant EQ208, [Glu208-->Gln] of alpha-amylase from Bacillus subtilis cocrystallized with, maltopentaose (G5) and acarbose has been determined by multiple, isomorphous replacement at 2.5 A resolution. Restrained crystallographic, refinement has resulted in an R-factor of 19.8% in the 7.0 to 2.5 A, resolution range. EQ208 consists of three domains containing a, (beta/alpha)8-barrel as observed in other alpha-amylases. Clear connected, density corresponding to a pentasaccharide was observed, which was, considered as the G5 molecule based on the high affinity of EQ208 for G5, that could replace pre-bound acarbose or a possible transglycosylation, product of acarbose. The conformation around the third, alpha-(1,4)-glucosidic bond makes a sharp ... [(full description)]

About this StructureAbout this Structure

1BAG is a [Single protein] structure of sequence from [Bacillus subtilis] with CA as [ligand]. Active as [Alpha-amylase], with EC number [3.2.1.1]. Structure known Active Sites: CA1, CA2 and CA3. Full crystallographic information is available from [OCA].

ReferenceReference

Crystal structure of a catalytic-site mutant alpha-amylase from Bacillus subtilis complexed with maltopentaose., Fujimoto Z, Takase K, Doui N, Momma M, Matsumoto T, Mizuno H, J Mol Biol. 1998 Mar 27;277(2):393-407. PMID:9514750

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