3vtk: Difference between revisions
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|PDB= 3vtk |SIZE=350|CAPTION= <scene name='initialview01'>3vtk</scene>, resolution 3.0Å | |PDB= 3vtk |SIZE=350|CAPTION= <scene name='initialview01'>3vtk</scene>, resolution 3.0Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=5IU:5-IODO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE'>5IU</scene>, <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Thymidine_kinase Thymidine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.21 2.7.1.21] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Thymidine_kinase Thymidine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.21 2.7.1.21] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3vtk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vtk OCA], [http://www.ebi.ac.uk/pdbsum/3vtk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3vtk RCSB]</span> | |||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
3VTK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | 3VTK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_1 Human herpesvirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VTK OCA]. | ||
==Reference== | ==Reference== | ||
The structures of thymidine kinase from herpes simplex virus type 1 in complex with substrates and a substrate analogue., Wild K, Bohner T, Folkers G, Schulz GE, Protein Sci. 1997 Oct;6(10):2097-106. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9336833 9336833] | The structures of thymidine kinase from herpes simplex virus type 1 in complex with substrates and a substrate analogue., Wild K, Bohner T, Folkers G, Schulz GE, Protein Sci. 1997 Oct;6(10):2097-106. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9336833 9336833] | ||
[[Category: Human herpesvirus | [[Category: Human herpesvirus 1]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thymidine kinase]] | [[Category: Thymidine kinase]] | ||
[[Category: Schulz, G E.]] | [[Category: Schulz, G E.]] | ||
[[Category: Wild, K.]] | [[Category: Wild, K.]] | ||
[[Category: additional thymidylate kinase activity]] | [[Category: additional thymidylate kinase activity]] | ||
[[Category: key enzyme in thymidine salvage pathway]] | [[Category: key enzyme in thymidine salvage pathway]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:36:34 2008'' | ||
Revision as of 05:36, 31 March 2008
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| , resolution 3.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Thymidine kinase, with EC number 2.7.1.21 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THYMIDINE KINASE FROM HERPES SIMPLEX VIRUS TYPE 1 IN COMPLEX WITH ADP AND 5-IODO-DEOXYURIDINE-MONOPHOSPHATE
OverviewOverview
Thymidine kinase from Herpes simplex virus type 1 (TK) was crystallized in an N-terminally truncated but fully active form. The structures of TK complexed with ADP at the ATP-site and deoxythymidine-5'-monophosphate (dTMP), deoxythymidine (dT), or idoxuridine-5'-phosphate (5-iodo-dUMP) at the substrate-site were refined to 2.75 A, 2.8 A, and 3.0 A resolution, respectively. TK catalyzes the phosphorylation of dT resulting in an ester, and the phosphorylation of dTMP giving rise to an anhydride. The presented TK structures indicate that there are only small differences between these two modes of action. Glu83 serves as a general base in the ester reaction. Arg163 parks at an internal aspartate during ester formation and binds the alpha-phosphate of dTMP during anhydride formation. The bound deoxythymidine leaves a 35 A3 cavity at position 5 of the base and two sequestered water molecules at position 2. Cavity and water molecules reduce the substrate specificity to such an extent that TK can phosphorylate various substrate analogues useful in pharmaceutical applications. TK is structurally homologous to the well-known nucleoside monophosphate kinases but contains large additional peptide segments.
About this StructureAbout this Structure
3VTK is a Single protein structure of sequence from Human herpesvirus 1. Full crystallographic information is available from OCA.
ReferenceReference
The structures of thymidine kinase from herpes simplex virus type 1 in complex with substrates and a substrate analogue., Wild K, Bohner T, Folkers G, Schulz GE, Protein Sci. 1997 Oct;6(10):2097-106. PMID:9336833
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