1rao: Difference between revisions
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|PDB= 1rao |SIZE=350|CAPTION= <scene name='initialview01'>1rao</scene>, resolution 1.56Å | |PDB= 1rao |SIZE=350|CAPTION= <scene name='initialview01'>1rao</scene>, resolution 1.56Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene> | |LIGAND= <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=HH2:6-HYDROXYMETHYLPTERIN-DIPHOSPHATE'>HH2</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/2-amino-4-hydroxy-6-hydroxymethyldihydropteridine_diphosphokinase 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.6.3 2.7.6.3] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/2-amino-4-hydroxy-6-hydroxymethyldihydropteridine_diphosphokinase 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.6.3 2.7.6.3] </span> | ||
|GENE= FOLK, B0142 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= FOLK, B0142 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1hka|1HKA]], [[1eqm|1EQM]], [[1eq0|1EQ0]], [[1q0n|1Q0N]], [[1ex8|1EX8]], [[1cbk|1CBK]], [[1dy3|1DY3]], [[1f9y|1F9Y]], [[1f9h|1F9H]], [[1g4c|1G4C]], [[1hq2|1HQ2]], [[1im6|1IM6]], [[1kbr|1KBR]], [[1rb0|1RB0]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rao OCA], [http://www.ebi.ac.uk/pdbsum/1rao PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rao RCSB]</span> | |||
}} | }} | ||
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[[Category: Blaszczyk, J.]] | [[Category: Blaszczyk, J.]] | ||
[[Category: Ji, X.]] | [[Category: Ji, X.]] | ||
[[Category: 6-hydroxymethyl-7,8-dihydropterin]] | |||
[[Category: 6-hydroxymethyl-7]] | |||
[[Category: 6-hydroxymethylpterin]] | [[Category: 6-hydroxymethylpterin]] | ||
[[Category: antimicrobial agent]] | [[Category: antimicrobial agent]] | ||
[[Category: catalytic mechanism]] | [[Category: catalytic mechanism]] | ||
| Line 43: | Line 43: | ||
[[Category: x-ray crystallography]] | [[Category: x-ray crystallography]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:25:31 2008'' | ||
Revision as of 23:25, 30 March 2008
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| , resolution 1.56Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | FOLK, B0142 (Escherichia coli) | ||||||
| Activity: | 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase, with EC number 2.7.6.3 | ||||||
| Related: | 1HKA, 1EQM, 1EQ0, 1Q0N, 1EX8, 1CBK, 1DY3, 1F9Y, 1F9H, 1G4C, 1HQ2, 1IM6, 1KBR, 1RB0
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF A TERNARY COMPLEX OF E. COLI HPPK WITH AMP AND 6-HYDROXYMETHYLPTERIN-DIPHOSPHATE AT 1.56 ANGSTROM RESOLUTION
OverviewOverview
6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) catalyzes the Mg(2+)-dependent pyrophosphoryl transfer from ATP to 6-hydroxymethyl-7,8-dihydropterin (HP). The reaction follows a bi-bi mechanism with ATP as the first substrate and AMP and HP pyrophosphate (HPPP) as the two products. HPPK is a key enzyme in the folate biosynthetic pathway and is essential for microorganisms but absent from mammals. For the HPPK-catalyzed pyrophosphoryl transfer, a reaction coordinate is constructed on the basis of the thermodynamic and transient kinetic data we reported previously, and the reaction trajectory is mapped out with five three-dimensional structures of the enzyme at various liganded states. The five structures are apo-HPPK (ligand-free enzyme), HPPK.MgATP(analog) (binary complex of HPPK with its first substrate) and HPPK.MgATP(analog).HP (ternary complex of HPPK with both substrates), which we reported previously, and HPPK.AMP.HPPP (ternary complex of HPPK with both product molecules) and HPPK.HPPP (binary complex of HPPK with one product), which we present in this study.
About this StructureAbout this Structure
1RAO is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Reaction trajectory of pyrophosphoryl transfer catalyzed by 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase., Blaszczyk J, Shi G, Li Y, Yan H, Ji X, Structure. 2004 Mar;12(3):467-75. PMID:15016362
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OCA- Pages with broken file links
- 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase
- Escherichia coli
- Single protein
- Blaszczyk, J.
- Ji, X.
- 6-hydroxymethyl-7,8-dihydropterin
- 6-hydroxymethylpterin
- Antimicrobial agent
- Catalytic mechanism
- Drug design
- Folate
- Hppk
- Product release
- Pterin
- Pyrophosphokinase
- Pyrophosphoryl transfer
- Substrate specificity
- Ternary complex
- X-ray crystallography