1xup

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[[Image:1xup.jpg|left|200px]]
[[Image:1xup.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1xup |SIZE=350|CAPTION= <scene name='initialview01'>1xup</scene>, resolution 2.75&Aring;
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The line below this paragraph, containing "STRUCTURE_1xup", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycerol_kinase Glycerol kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.30 2.7.1.30] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= glpK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=37734 Enterococcus casseliflavus])
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-->
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|DOMAIN=
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{{STRUCTURE_1xup| PDB=1xup | SCENE= }}
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|RELATEDENTRY=[[1r59|1R59]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xup OCA], [http://www.ebi.ac.uk/pdbsum/1xup PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xup RCSB]</span>
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}}
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'''ENTEROCOCCUS CASSELIFLAVUS GLYCEROL KINASE COMPLEXED WITH GLYCEROL'''
'''ENTEROCOCCUS CASSELIFLAVUS GLYCEROL KINASE COMPLEXED WITH GLYCEROL'''
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[[Category: Paulo, J.]]
[[Category: Paulo, J.]]
[[Category: Yeh, J I.]]
[[Category: Yeh, J I.]]
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[[Category: transferase]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:31:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:54:54 2008''
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Revision as of 12:31, 3 May 2008

Image:1xup.jpg

Template:STRUCTURE 1xup

ENTEROCOCCUS CASSELIFLAVUS GLYCEROL KINASE COMPLEXED WITH GLYCEROL


Overview

The first structure of a glycerol kinase from a Gram-positive organism, Enterococcus casseliflavus, has been determined to 2.8 A resolution in the presence of glycerol and to 2.5 A resolution in the absence of substrate. The substrate-induced closure of 7 degrees is significantly smaller than that reported for hexokinase, a model for substrate-mediated domain closure that has been proposed for glycerol kinase. Despite the 78% level of sequence identity and conformational similarity in the catalytic cleft regions of the En. casseliflavus and Escherichia coli glycerol kinases, remarkable structural differences have now been identified. These differences correlate well with their divergent regulatory schemes of activation by phosphorylation in En. casseliflavus and allosteric inhibition in E. coli. On the basis of our structural results, we propose a mechanism by which the phosphorylation of a histidyl residue located 25 A from the active site results in a 10-15-fold increase in the activity of the enterococcal glycerol kinase.

About this Structure

1XUP is a Single protein structure of sequence from Enterococcus casseliflavus. Full crystallographic information is available from OCA.

Reference

Structures of enterococcal glycerol kinase in the absence and presence of glycerol: correlation of conformation to substrate binding and a mechanism of activation by phosphorylation., Yeh JI, Charrier V, Paulo J, Hou L, Darbon E, Claiborne A, Hol WG, Deutscher J, Biochemistry. 2004 Jan 20;43(2):362-73. PMID:14717590 Page seeded by OCA on Sat May 3 15:31:58 2008

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