1esw: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1esw.jpg|left|200px]]<br /><applet load="1esw" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1esw, resolution 1.90&Aring;" />
-'''X-RAY STRUCTURE OF ACARBOSE BOUND TO AMYLOMALTASE FROM THERMUS AQUATICUS. IMPLICATIONS FOR THE SYNTHESIS OF LARGE CYCLIC GLUCANS'''<br />
-==Overview==
+==X-RAY STRUCTURE OF ACARBOSE BOUND TO AMYLOMALTASE FROM THERMUS AQUATICUS. IMPLICATIONS FOR THE SYNTHESIS OF LARGE CYCLIC GLUCANS==
-As a member of the alpha-amylase superfamily of enzymes, amylomaltase, catalyzes either the transglycosylation from one alpha-1,4 glucan to, another or an intramolecular cyclization. The latter reaction is typical, for cyclodextrin glucanotransferases. In contrast to these enzymes, amylomaltase catalyzes the formation of cyclic glucans with a degree of, polymerization larger than 22. To characterize the factors that determine, the size of the synthesized cycloamyloses, we have analyzed the X-ray, structure of amylomaltase from Thermus aquaticus in complex with the, inhibitor acarbose, a maltotetraose derivative, at 1.9 A resolution. Two, acarbose molecules are bound to the enzyme, one in the active site groove, at subsite -3 to +1 and a second one approximately 14 A away from the, nonreducing end of the acarbose bound to the catalytic site. The inhibitor, bound to the catalytic site occupies subsites -3 to +1. Unlike the, situation in other enzymes of the alpha-amylase family, the inhibitor is, not processed and the inhibitory cyclitol ring of acarbose, which mimicks, the half chair conformation of the transition state, does not bind to, catalytic subsite -1. The minimum ring size of cycloamyloses produced by, this enzyme is proposed to be determined by the distance of the specific, substrate binding sites at the active site and near Tyr54 and by the size, of the 460s loop. The 250s loop might be involved in binding of the, substrate at the reducing end of the scissile bond.
+<StructureSection load='1esw' size='340' side='right'caption='[[1esw]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+== Structural highlights ==
-==About this Structure==
+<table><tr><td colspan='2'>[[1esw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ESW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ESW FirstGlance]. <br>
-ESW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus] with ACR and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/4-alpha-glucanotransferase 4-alpha-glucanotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.25 2.4.1.25] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ESW OCA].
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AC1:6-METHYL-5-(4,5,6-TRIHYDROXY-3-HYDROXYMETHYL-CYCLOHEX-2-ENYLAMINO)-TETRAHYDRO-PYRAN-2,3,4-TRIOL'>AC1</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900007:alpha-acarbose'>PRD_900007</scene></td></tr>
-==Reference==
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1esw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1esw OCA], [https://pdbe.org/1esw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1esw RCSB], [https://www.ebi.ac.uk/pdbsum/1esw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1esw ProSAT]</span></td></tr>
-X-ray structure of acarbose bound to amylomaltase from Thermus aquaticus. Implications for the synthesis of large cyclic glucans., Przylas I, Terada Y, Fujii K, Takaha T, Saenger W, Strater N, Eur J Biochem. 2000 Dec;267(23):6903-13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11082203 11082203]
+</table>
-[[Category: 4-alpha-glucanotransferase]]
+== Function ==
-[[Category: Single protein]]
+[https://www.uniprot.org/uniprot/MALQ_THETH MALQ_THETH]
+== 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/es/1esw_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=1esw ConSurf].
+<div style="clear:both"></div>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Thermus aquaticus]]
-[[Category: Fujii, K.]]
+[[Category: Fujii K]]
-[[Category: Przylas, I.]]
+[[Category: Przylas I]]
-[[Category: Saenger, W.]]
+[[Category: Saenger W]]
-[[Category: Straeter, N.]]
+[[Category: Straeter N]]
-[[Category: Takaha, T.]]
+[[Category: Takaha T]]
-[[Category: Terada, Y.]]
+[[Category: Terada Y]]
-[[Category: ACR]]
-[[Category: EDO]]
-[[Category: (beta]]
-[[Category: acarbose]]
-[[Category: alpha)8-barrel]]
-[[Category: alpha-amylase family]]
-[[Category: glucanotransferase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:17:24 2007''