1p74: Difference between revisions
No edit summary |
No edit summary |
||
| Line 5: | Line 5: | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Shikimate_dehydrogenase Shikimate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.25 1.1.1.25] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Shikimate_dehydrogenase Shikimate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.25 1.1.1.25] </span> | ||
|GENE= AROE OR HI0655 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 Haemophilus influenzae]) | |GENE= AROE OR HI0655 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 Haemophilus influenzae]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1p77|1P77]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p74 OCA], [http://www.ebi.ac.uk/pdbsum/1p74 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1p74 RCSB]</span> | |||
}} | }} | ||
| Line 32: | Line 35: | ||
[[Category: shikimate dehydrogenase]] | [[Category: shikimate dehydrogenase]] | ||
''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 22:55:48 2008'' | ||
Revision as of 19:55, 30 March 2008
| |||||||||||||
| 1p74, resolution 2.40Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Gene: | AROE OR HI0655 (Haemophilus influenzae) | ||||||||||||
| Activity: | Shikimate dehydrogenase, with EC number 1.1.1.25 | ||||||||||||
| Related: | 1P77
| ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
CRYSTAL STRUCTURE OF SHIKIMATE DEHYDROGENASE (AROE) FROM HAEMOPHILUS INFLUENZAE
Overview
Shikimate dehydrogenase catalyzes the NADPH-dependent reversible reduction of 3-dehydroshikimate to shikimate. We report the first X-ray structure of shikimate dehydrogenase from Haemophilus influenzae to 2.4-A resolution and its complex with NADPH to 1.95-A resolution. The molecule contains two domains, a catalytic domain with a novel open twisted alpha/beta motif and an NADPH binding domain with a typical Rossmann fold. The enzyme contains a unique glycine-rich P-loop with a conserved sequence motif, GAGGXX, that results in NADPH adopting a nonstandard binding mode with the nicotinamide and ribose moieties disordered in the binary complex. A deep pocket with a narrow entrance between the two domains, containing strictly conserved residues primarily contributed by the catalytic domain, is identified as a potential 3-dehydroshikimate binding pocket. The flexibility of the nicotinamide mononucleotide portion of NADPH may be necessary for the substrate 3-dehydroshikimate to enter the pocket and for the release of the product shikimate.
About this Structure
1P74 is a Single protein structure of sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.
Reference
The crystal structure of shikimate dehydrogenase (AroE) reveals a unique NADPH binding mode., Ye S, Von Delft F, Brooun A, Knuth MW, Swanson RV, McRee DE, J Bacteriol. 2003 Jul;185(14):4144-51. PMID:12837789
Page seeded by OCA on Sun Mar 30 22:55:48 2008
