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.


1xii

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:50, 14 February 2024) (edit) (undo)
 
(13 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1xii.jpg|left|200px]]
 
-
{{Structure
+
==MODES OF BINDING SUBSTRATES AND THEIR ANALOGUES TO THE ENZYME D-XYLOSE ISOMERASE==
-
|PDB= 1xii |SIZE=350|CAPTION= <scene name='initialview01'>1xii</scene>, resolution 1.7&Aring;
+
<StructureSection load='1xii' size='340' side='right'caption='[[1xii]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=XUL:D-XYLULOSE'>XUL</scene> and <scene name='pdbligand=MN:MANGANESE (II) ION'>MN</scene>
+
<table><tr><td colspan='2'>[[1xii]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_rubiginosus Streptomyces rubiginosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XII OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XII FirstGlance]. <br>
-
|ACTIVITY= [http://en.wikipedia.org/wiki/Xylose_isomerase Xylose isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.5 5.3.1.5]
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
-
|GENE=
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=XUL:D-XYLULOSE'>XUL</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=1xii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xii OCA], [https://pdbe.org/1xii PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xii RCSB], [https://www.ebi.ac.uk/pdbsum/1xii PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xii ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/XYLA_STRRU XYLA_STRRU] Involved in D-xylose catabolism.
 +
== 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/xi/1xii_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=1xii ConSurf].
 +
<div style="clear:both"></div>
-
'''MODES OF BINDING SUBSTRATES AND THEIR ANALOGUES TO THE ENZYME D-XYLOSE ISOMERASE'''
+
==See Also==
-
 
+
*[[D-xylose isomerase 3D structures|D-xylose isomerase 3D structures]]
-
 
+
__TOC__
-
==Overview==
+
</StructureSection>
-
Studies of binding of substrates and inhibitors of the enzyme D-xylose isomerase show, from X-ray diffraction data at 1.6-1.9 A resolution, that there are a variety of binding modes. These vary in the manner in which the substrate or its analogue extend, on binding, across the carboxy end of the (betaalpha)(8)-barrel structure. These binding sites are His54 and the metal ion (magnesium or manganese) that is held in place by Glul81, Asp245, Glu217 and Asp287. Possible catalytic groups have been identified in proposed mechanisms and their role in the binding of ligands is illustrated.
+
[[Category: Large Structures]]
-
 
+
-
==About this Structure==
+
-
1XII is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_rubiginosus Streptomyces rubiginosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XII OCA].
+
-
 
+
-
==Reference==
+
-
Modes of binding substrates and their analogues to the enzyme D-xylose isomerase., Carrell HL, Hoier H, Glusker JP, Acta Crystallogr D Biol Crystallogr. 1994 Mar 1;50(Pt 2):113-23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15299449 15299449]
+
-
[[Category: Single protein]]
+
[[Category: Streptomyces rubiginosus]]
[[Category: Streptomyces rubiginosus]]
-
[[Category: Xylose isomerase]]
+
[[Category: Carrell HL]]
-
[[Category: Carrell, H L.]]
+
[[Category: Glusker JP]]
-
[[Category: Glusker, J P.]]
+
-
[[Category: MN]]
+
-
[[Category: XUL]]
+
-
[[Category: isomerase(intramolecular oxidoreductse)]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:10:16 2008''
+

Current revision

MODES OF BINDING SUBSTRATES AND THEIR ANALOGUES TO THE ENZYME D-XYLOSE ISOMERASE

PDB ID 1xii

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools