1rb0
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=HH2:6-HYDROXYMETHYLPTERIN-DIPHOSPHATE'>HH2</scene> | |LIGAND= <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]], [[1rao|1RAO]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rb0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rb0 OCA], [http://www.ebi.ac.uk/pdbsum/1rb0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rb0 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: 8-dihydropterin]] | ||
[[Category: antimicrobial agent]] | [[Category: antimicrobial agent]] | ||
[[Category: binary complex]] | [[Category: binary complex]] | ||
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[[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 23:25:38 2008'' |
Revision as of 20:25, 30 March 2008
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| , resolution 1.35Å | |||||||
|---|---|---|---|---|---|---|---|
| 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, 1RAO
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF A BINARY COMPLEX OF E. COLI HPPK WITH 6-HYDROXYMETHYLPTERIN-DIPHOSPHATE AT 1.35 ANGSTROM RESOLUTION
Overview
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 Structure
1RB0 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Mar 30 23:25:38 2008
Categories: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase | Escherichia coli | Single protein | Blaszczyk, J. | Ji, X. | 6-hydroxymethyl-7,8-dihydropterin | 6-hydroxymethylpterin | Antimicrobial agent | Binary complex | Catalytic mechanism | Drug design | Folate | Hppk | Product release | Pterin | Pyrophosphokinase | Pyrophosphoryl transfer | Substrate specificity | Ternary complex | X-ray crystallography
