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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[[Image:1bag.gif|left|200px]]<br />
<applet load="1bag" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1bag, resolution 2.5&Aring;" />
'''ALPHA-AMYLASE FROM BACILLUS SUBTILIS COMPLEXED WITH MALTOPENTAOSE'''<br />


==Overview==
==ALPHA-AMYLASE FROM BACILLUS SUBTILIS COMPLEXED WITH MALTOPENTAOSE==
The X-ray crystal structure of a catalytic-site mutant EQ208, [Glu208--&gt;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 ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9514750 (full description)]]
<StructureSection load='1bag' size='340' side='right'caption='[[1bag]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1bag]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BAG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BAG FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bag OCA], [https://pdbe.org/1bag PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bag RCSB], [https://www.ebi.ac.uk/pdbsum/1bag PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bag ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AMY_BACSU AMY_BACSU]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ba/1bag_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1bag ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
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]].
*[[Amylase 3D structures|Amylase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Doui, N.]]
[[Category: Doui N]]
[[Category: Fujimoto, Z.]]
[[Category: Fujimoto Z]]
[[Category: Mizuno, H.]]
[[Category: Mizuno H]]
[[Category: Takase, K.]]
[[Category: Takase K]]
[[Category: CA]]
[[Category: alpha-amylase]]
[[Category: bacillus subtilis]]
[[Category: catalytic-site mutant]]
[[Category: maltopentaose]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 20:08:06 2007''

Latest revision as of 06:34, 7 February 2024

ALPHA-AMYLASE FROM BACILLUS SUBTILIS COMPLEXED WITH MALTOPENTAOSE

1bag, resolution 2.50Å

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