1rfv: Difference between revisions
New page: left|200px<br /><applet load="1rfv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rfv, resolution 2.8Å" /> '''Crystal structure of ... |
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[[Image:1rfv.jpg|left|200px]]<br /><applet load="1rfv" size=" | [[Image:1rfv.jpg|left|200px]]<br /><applet load="1rfv" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1rfv, resolution 2.8Å" /> | caption="1rfv, resolution 2.8Å" /> | ||
'''Crystal structure of pyridoxal kinase complexed with ADP'''<br /> | '''Crystal structure of pyridoxal kinase complexed with ADP'''<br /> | ||
==Overview== | ==Overview== | ||
To understand the processes involved in the catalytic mechanism of | 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== | ==About this Structure== | ||
1RFV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ovis_aries Ovis aries] with ZN and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | 1RFV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ovis_aries Ovis aries] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RFV OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Jiang, T.]] | [[Category: Jiang, T.]] | ||
[[Category: Li, M | [[Category: Li, M H.]] | ||
[[Category: Liang, D | [[Category: Liang, D C.]] | ||
[[Category: ADP]] | [[Category: ADP]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: transferase]] | [[Category: transferase]] | ||
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Revision as of 15:50, 21 February 2008
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Crystal structure of pyridoxal kinase complexed with ADP
OverviewOverview
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 StructureAbout this Structure
1RFV is a Single protein structure of sequence from Ovis aries with and as ligands. Active as Pyridoxal kinase, with EC number 2.7.1.35 Full crystallographic information is available from OCA.
ReferenceReference
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
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