2gve

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[[Image:2gve.gif|left|200px]]<br /><applet load="2gve" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2gve.gif|left|200px]]
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caption="2gve, resolution 2.2&Aring;" />
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'''Time-of-Flight Neutron Diffraction Structure of D-Xylose Isomerase'''<br />
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{{Structure
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|PDB= 2gve |SIZE=350|CAPTION= <scene name='initialview01'>2gve</scene>, resolution 2.2&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene> and <scene name='pdbligand=DOD:DEUTERATED WATER'>DOD</scene>
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|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]
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|GENE=
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}}
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'''Time-of-Flight Neutron Diffraction Structure of D-Xylose Isomerase'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2GVE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_rubiginosus Streptomyces rubiginosus] with <scene name='pdbligand=CO:'>CO</scene> and <scene name='pdbligand=DOD:'>DOD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GVE OCA].
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2GVE 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=2GVE OCA].
==Reference==
==Reference==
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Locating active-site hydrogen atoms in D-xylose isomerase: time-of-flight neutron diffraction., Katz AK, Li X, Carrell HL, Hanson BL, Langan P, Coates L, Schoenborn BP, Glusker JP, Bunick GJ, Proc Natl Acad Sci U S A. 2006 May 30;103(22):8342-7. Epub 2006 May 17. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16707576 16707576]
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Locating active-site hydrogen atoms in D-xylose isomerase: time-of-flight neutron diffraction., Katz AK, Li X, Carrell HL, Hanson BL, Langan P, Coates L, Schoenborn BP, Glusker JP, Bunick GJ, Proc Natl Acad Sci U S A. 2006 May 30;103(22):8342-7. Epub 2006 May 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16707576 16707576]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Streptomyces rubiginosus]]
[[Category: Streptomyces rubiginosus]]
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[[Category: CO]]
[[Category: CO]]
[[Category: DOD]]
[[Category: DOD]]
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[[Category: protonation states of residues]]
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[[Category: protonation states of residue]]
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[[Category: tim barrel-beta-alpha-barrels]]
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[[Category: tim barrel-beta-alpha-barrel]]
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[[Category: two metal binding sites]]
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[[Category: two metal binding site]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:35:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:09:37 2008''

Revision as of 15:09, 20 March 2008


PDB ID 2gve

Drag the structure with the mouse to rotate
, resolution 2.2Å
Ligands: and
Activity: Xylose isomerase, with EC number 5.3.1.5
Coordinates: save as pdb, mmCIF, xml



Time-of-Flight Neutron Diffraction Structure of D-Xylose Isomerase


Overview

Time-of-flight neutron diffraction has been used to locate hydrogen atoms that define the ionization states of amino acids in crystals of D-xylose isomerase. This enzyme, from Streptomyces rubiginosus, is one of the largest enzymes studied to date at high resolution (1.8 A) by this method. We have determined the position and orientation of a metal ion-bound water molecule that is located in the active site of the enzyme; this water has been thought to be involved in the isomerization step in which D-xylose is converted to D-xylulose or D-glucose to D-fructose. It is shown to be water (rather than a hydroxyl group) under the conditions of measurement (pH 8.0). Our analyses also reveal that one lysine probably has an -NH(2)-terminal group (rather than NH(3)(+)). The ionization state of each histidine residue also was determined. High-resolution x-ray studies (at 0.94 A) indicate disorder in some side chains when a truncated substrate is bound and suggest how some side chains might move during catalysis. This combination of time-of-flight neutron diffraction and x-ray diffraction can contribute greatly to the elucidation of enzyme mechanisms.

About this Structure

2GVE is a Single protein structure of sequence from Streptomyces rubiginosus. Full crystallographic information is available from OCA.

Reference

Locating active-site hydrogen atoms in D-xylose isomerase: time-of-flight neutron diffraction., Katz AK, Li X, Carrell HL, Hanson BL, Langan P, Coates L, Schoenborn BP, Glusker JP, Bunick GJ, Proc Natl Acad Sci U S A. 2006 May 30;103(22):8342-7. Epub 2006 May 17. PMID:16707576

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