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.


1ogo

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (05:47, 17 April 2024) (edit) (undo)
 
(17 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1ogo.gif|left|200px]]<br /><applet load="1ogo" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1ogo, resolution 1.65&Aring;" />
 
-
'''DEX49A FROM PENICILLIUM MINIOLUTEUM COMPLEX WITH ISOMALTOSE'''<br />
 
-
==Overview==
+
==Dex49A from Penicillium minioluteum complex with isomaltose==
-
Dextranase catalyzes the hydrolysis of the alpha-1,6-glycosidic linkage in, dextran polymers. The structure of dextranase, Dex49A, from Penicillium, minioluteum was solved in the apo-enzyme and product-bound forms. The main, domain of the enzyme is a right-handed parallel beta helix, which is, connected to a beta sandwich domain at the N terminus. In the structure of, the product complex, isomaltose was found to bind in a crevice on the, surface of the enzyme. The glycosidic oxygen of the glucose unit in, subsite +1 forms a hydrogen bond to the suggested catalytic acid, Asp395., By NMR spectroscopy the reaction course was shown to occur with net, inversion at the anomeric carbon, implying a single displacement, mechanism. Both Asp376 and Asp396 are suitably positioned to activate the, water molecule that performs the nucleophilic attack. A new clan that, links glycoside hydrolase families 28 and 49 is suggested.
+
<StructureSection load='1ogo' size='340' side='right'caption='[[1ogo]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
-
 
+
== Structural highlights ==
-
==About this Structure==
+
<table><tr><td colspan='2'>[[1ogo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Talaromyces_minioluteus Talaromyces minioluteus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OGO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OGO FirstGlance]. <br>
-
1OGO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Penicillium_minioluteum Penicillium minioluteum]. Active as [http://en.wikipedia.org/wiki/Dextranase Dextranase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.11 3.2.1.11] Known structural/functional Site: <scene name='pdbsite=CAT:Glc Binding Site For Chain X'>CAT</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OGO 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]] 1.65&#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=GLC:ALPHA-D-GLUCOSE'>GLC</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=1ogo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ogo OCA], [https://pdbe.org/1ogo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ogo RCSB], [https://www.ebi.ac.uk/pdbsum/1ogo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ogo ProSAT]</span></td></tr>
-
Dextranase from Penicillium minioluteum: reaction course, crystal structure, and product complex., Larsson AM, Andersson R, Stahlberg J, Kenne L, Jones TA, Structure. 2003 Sep;11(9):1111-21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12962629 12962629]
+
</table>
-
[[Category: Dextranase]]
+
== Function ==
-
[[Category: Penicillium minioluteum]]
+
[https://www.uniprot.org/uniprot/DEXT_TALMI DEXT_TALMI]
-
[[Category: Single protein]]
+
== Evolutionary Conservation ==
-
[[Category: Jones, T.A.]]
+
[[Image:Consurf_key_small.gif|200px|right]]
-
[[Category: Larsson, A.M.]]
+
Check<jmol>
-
[[Category: Stahlberg, J.]]
+
<jmolCheckbox>
-
[[Category: dextran degradation]]
+
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/og/1ogo_consurf.spt"</scriptWhenChecked>
-
[[Category: glycosidase]]
+
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
-
[[Category: hydrolase]]
+
<text>to colour the structure by Evolutionary Conservation</text>
-
 
+
</jmolCheckbox>
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 17:42:23 2007''
+
</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=1ogo ConSurf].
 +
<div style="clear:both"></div>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
 +
[[Category: Talaromyces minioluteus]]
 +
[[Category: Jones TA]]
 +
[[Category: Larsson AM]]
 +
[[Category: Stahlberg J]]

Current revision

Dex49A from Penicillium minioluteum complex with isomaltose

PDB ID 1ogo

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ogo"
Personal tools