2glk
From Proteopedia
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| - | [[Image:2glk.gif|left|200px]] | + | [[Image:2glk.gif|left|200px]] |
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| - | '''High-resolution study of D-Xylose isomerase, 0.94A resolution.''' | + | {{Structure |
| + | |PDB= 2glk |SIZE=350|CAPTION= <scene name='initialview01'>2glk</scene>, resolution 0.94Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''High-resolution study of D-Xylose isomerase, 0.94A resolution.''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2GLK is a [ | + | 2GLK 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=2GLK OCA]. |
==Reference== | ==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:[http:// | + | 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: GOL]] | [[Category: GOL]] | ||
[[Category: MN]] | [[Category: MN]] | ||
| - | [[Category: beta-alpha- | + | [[Category: beta-alpha-barrel]] |
[[Category: tim barrel]] | [[Category: tim barrel]] | ||
| - | [[Category: two metal binding | + | [[Category: two metal binding site]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:06:07 2008'' |
Revision as of 15:06, 20 March 2008
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| , resolution 0.94Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Xylose isomerase, with EC number 5.3.1.5 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
High-resolution study of D-Xylose isomerase, 0.94A resolution.
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
2GLK 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
Page seeded by OCA on Thu Mar 20 17:06:07 2008
