This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1mwo

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1mwo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mwo, resolution 2.2&Aring;" /> '''Crystal Structure Ana...)
Current revision (08:42, 10 April 2024) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1mwo.jpg|left|200px]]<br /><applet load="1mwo" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1mwo, resolution 2.2&Aring;" />
 
-
'''Crystal Structure Analysis of the Hyperthermostable Pyrocoocus woesei alpha-amylase'''<br />
 
-
==Overview==
+
==Crystal Structure Analysis of the Hyperthermostable Pyrocoocus woesei alpha-amylase==
-
The crystal structure of the alpha-amylase from the hyperthermophilic, archaeon Pyrococcus woesei was solved in the presence of three inhibitors:, acarbose, Tris, and zinc. In the absence of exogenous metals, this, alpha-amylase bound 1 and 4 molar eq of zinc and calcium, respectively., The structure reveals a novel, activating, two-metal (Ca,Zn)-binding site, and a second inhibitory zinc-binding site that is found in the -1, sugar-binding pocket within the active site. The data resolve the apparent, paradox between the zinc requirement for catalytic activity and its strong, inhibitory effect when added in molar excess. They provide a rationale as, to why this alpha-amylase, in contrast to commercially available, alpha-amylases, does not require the addition of metal ions for full, catalytic activity, suggesting it as an ideal target to maximize the, efficiency of industrial processes like liquefaction of starch.
+
<StructureSection load='1mwo' size='340' side='right'caption='[[1mwo]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1mwo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_woesei Pyrococcus woesei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MWO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MWO 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]] 2.2&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1mwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mwo OCA], [https://pdbe.org/1mwo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mwo RCSB], [https://www.ebi.ac.uk/pdbsum/1mwo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mwo ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/Q7LYT7_PYRWO Q7LYT7_PYRWO]
 +
== 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/mw/1mwo_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=1mwo ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1MWO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_woesei Pyrococcus woesei] with ZN and CA as [http://en.wikipedia.org/wiki/ligands ligands]. 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MWO OCA].
+
*[[Amylase 3D structures|Amylase 3D structures]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
Differential regulation of a hyperthermophilic alpha-amylase with a novel (Ca,Zn) two-metal center by zinc., Linden A, Mayans O, Meyer-Klaucke W, Antranikian G, Wilmanns M, J Biol Chem. 2003 Mar 14;278(11):9875-84. Epub 2002 Dec 12. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12482867 12482867]
+
[[Category: Large Structures]]
-
[[Category: Alpha-amylase]]
+
[[Category: Pyrococcus woesei]]
[[Category: Pyrococcus woesei]]
-
[[Category: Single protein]]
+
[[Category: Antranikian G]]
-
[[Category: Antranikian, G.]]
+
[[Category: Linden A]]
-
[[Category: Linden, A.]]
+
[[Category: Mayans O]]
-
[[Category: Mayans, O.]]
+
[[Category: Meyer-Klaucke W]]
-
[[Category: Meyer-Klaucke, W.]]
+
[[Category: Wilmanns M]]
-
[[Category: Wilmanns, M.]]
+
-
[[Category: CA]]
+
-
[[Category: ZN]]
+
-
[[Category: (beta/alpha)8-barrel]]
+
-
[[Category: alpha-amylase]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 22:07:42 2007''
+

Current revision

Crystal Structure Analysis of the Hyperthermostable Pyrocoocus woesei alpha-amylase

PDB ID 1mwo

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools