1rfv

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[[Image:1rfv.jpg|left|200px]]
[[Image:1rfv.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1rfv |SIZE=350|CAPTION= <scene name='initialview01'>1rfv</scene>, resolution 2.8&Aring;
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The line below this paragraph, containing "STRUCTURE_1rfv", 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=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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/Pyridoxal_kinase Pyridoxal kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.35 2.7.1.35] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1rfv| PDB=1rfv | SCENE= }}
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|RELATEDENTRY=[[1lhp|1LHP]], [[1lhr|1LHR]], [[1rft|1RFT]], [[1rfu|1RFU]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rfv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rfv OCA], [http://www.ebi.ac.uk/pdbsum/1rfv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rfv RCSB]</span>
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}}
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'''Crystal structure of pyridoxal kinase complexed with ADP'''
'''Crystal structure of pyridoxal kinase complexed with ADP'''
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[[Category: Li, M H.]]
[[Category: Li, M H.]]
[[Category: Liang, D C.]]
[[Category: Liang, D C.]]
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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 07:26:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:27:37 2008''
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Revision as of 04:26, 3 May 2008

Image:1rfv.jpg

Template:STRUCTURE 1rfv

Crystal structure of pyridoxal kinase complexed with ADP


Overview

To understand the processes involved in the catalytic mechanism of pyridoxal kinase (PLK),1 we determined the crystal structures of PLK.AMP-PCP-pyridoxamine, PLK.ADP.PLP, and PLK.ADP complexes. Comparisons of these structures have revealed that PLK exhibits different conformations during its catalytic process. After the binding of AMP-PCP (an analogue that replaced ATP) and pyridoxamine to PLK, this enzyme retains a conformation similar to that of the PLK.ATP complex. The distance between the reacting groups of the two substrates is 5.8 A apart, indicating that the position of ATP is not favorable to spontaneous transfer of its phosphate group. However, the structure of PLK.ADP.PLP complex exhibited significant changes in both the conformation of the enzyme and the location of the ligands at the active site. Therefore, it appears that after binding of both substrates, the enzyme-substrate complex requires changes in the protein structure to enable the transfer of the phosphate group from ATP to vitamin B(6). Furthermore, a conformation of the enzyme-substrate complex before the transition state of the enzymatic reaction was also hypothesized.

About this Structure

1RFV is a Single protein structure of sequence from Ovis aries. Full crystallographic information is available from OCA.

Reference

Conformational changes in the reaction of pyridoxal kinase., Li MH, Kwok F, Chang WR, Liu SQ, Lo SC, Zhang JP, Jiang T, Liang DC, J Biol Chem. 2004 Apr 23;279(17):17459-65. Epub 2004 Jan 13. PMID:14722069 Page seeded by OCA on Sat May 3 07:26:58 2008

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