1ru1: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1ru1.jpg|left|200px]] | [[Image:1ru1.jpg|left|200px]] | ||
'''CRYSTAL STRUCTURE OF A TERNARY COMPLEX OF E. COLI HPPK(V83G/DEL84-89) WITH MGAMPCPP AND 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN AT 1.40 ANGSTROM RESOLUTION (MONOCLINIC FORM)''' | {{Structure | ||
|PDB= 1ru1 |SIZE=350|CAPTION= <scene name='initialview01'>1ru1</scene>, resolution 1.40Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene> and <scene name='pdbligand=PH2:2-AMINO-6-HYDROXYMETHYL-7,8-DIHYDRO-3H-PTERIDIN-4-ONE'>PH2</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] | |||
|GENE= FOLK, B0142 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |||
}} | |||
'''CRYSTAL STRUCTURE OF A TERNARY COMPLEX OF E. COLI HPPK(V83G/DEL84-89) WITH MGAMPCPP AND 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN AT 1.40 ANGSTROM RESOLUTION (MONOCLINIC FORM)''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1RU1 is a [ | 1RU1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RU1 OCA]. | ||
==Reference== | ==Reference== | ||
Essential roles of a dynamic loop in the catalysis of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase., Blaszczyk J, Li Y, Wu Y, Shi G, Ji X, Yan H, Biochemistry. 2004 Feb 17;43(6):1469-77. PMID:[http:// | Essential roles of a dynamic loop in the catalysis of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase., Blaszczyk J, Li Y, Wu Y, Shi G, Ji X, Yan H, Biochemistry. 2004 Feb 17;43(6):1469-77. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14769023 14769023] | ||
[[Category: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase]] | [[Category: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| Line 32: | Line 41: | ||
[[Category: x-ray crystallography]] | [[Category: x-ray crystallography]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:56:17 2008'' | ||
Revision as of 14:56, 20 March 2008
| |||||||
| , resolution 1.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , and | ||||||
| Gene: | FOLK, B0142 (Escherichia coli) | ||||||
| Activity: | 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase, with EC number 2.7.6.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF A TERNARY COMPLEX OF E. COLI HPPK(V83G/DEL84-89) WITH MGAMPCPP AND 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN AT 1.40 ANGSTROM RESOLUTION (MONOCLINIC FORM)
OverviewOverview
6-Hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) catalyzes the transfer of pyrophosphoryl group from ATP to 6-hydroxymethyl-7,8-dihydropterin (HP) following an ordered bi-bi mechanism with ATP as the first substrate. The rate-limiting step of the reaction is product release, and the complete active center is assembled and sealed only upon the binding of both ATP and HP. The assembly of the active center involves large conformational changes in three catalytic loops, among which loop 3 undergoes the most dramatic and unusual changes. To investigate the roles of loop 3 in catalysis, we have made a deletion mutant, which has been investigated by biochemical and X-ray crystallographic analysis. The biochemical data showed that the deletion mutation does not have significant effects on the dissociation constants or the rate constants for the binding of the first substrate MgATP or its analogues. The dissociation constant of HP for the mutant increases by a factor of approximately 100, which is due to a large increase in the dissociation rate constant. The deletion mutation causes a shift of the rate-limiting step in the reaction and a decrease in the rate constant for the chemical step by a factor of approximately 1.1 x 10(5). The crystal structures revealed that the deletion mutation does not affect protein folding, but the catalytic center of the mutant is not fully assembled even upon the formation of the ternary complex and is not properly sealed. The results together suggest that loop 3 is dispensable for the folding of the protein and the binding of the first substrate MgATP, but is required for the assembling and sealing of the active center. The loop plays an important role in the stabilization of the ternary complex and is critical for catalysis.
About this StructureAbout this Structure
1RU1 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Essential roles of a dynamic loop in the catalysis of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase., Blaszczyk J, Li Y, Wu Y, Shi G, Ji X, Yan H, Biochemistry. 2004 Feb 17;43(6):1469-77. PMID:14769023
Page seeded by OCA on Thu Mar 20 13:56:17 2008
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase
- Escherichia coli
- Single protein
- Blaszczyk, J.
- Ji, X.
- APC
- CL
- MG
- PH2
- 6-hydroxymethyl-7
- 8-dihydropterin
- Antimicrobial agent
- Deletion mutant
- Drug design
- Folate
- Hppk
- Pterin
- Pyrophosphokinase
- Pyrophosphoryl transfer
- X-ray crystallography