2fp1: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 2fp1 |SIZE=350|CAPTION= <scene name='initialview01'>2fp1</scene>, resolution 1.55Å | |PDB= 2fp1 |SIZE=350|CAPTION= <scene name='initialview01'>2fp1</scene>, resolution 1.55Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=PB:LEAD (II) ION'>PB</scene> | |LIGAND= <scene name='pdbligand=PB:LEAD+(II)+ION'>PB</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Chorismate_mutase Chorismate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.5 5.4.99.5] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Chorismate_mutase Chorismate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.5 5.4.99.5] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[2fp2|2FP2]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fp1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fp1 OCA], [http://www.ebi.ac.uk/pdbsum/2fp1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fp1 RCSB]</span> | |||
}} | }} | ||
| Line 29: | Line 32: | ||
[[Category: Okvist, M.]] | [[Category: Okvist, M.]] | ||
[[Category: Sasso, S.]] | [[Category: Sasso, S.]] | ||
[[Category: alpha-helical]] | [[Category: alpha-helical]] | ||
''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 03:05:49 2008'' | ||
Revision as of 03:05, 31 March 2008
| |||||||
| , resolution 1.55Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Chorismate mutase, with EC number 5.4.99.5 | ||||||
| Related: | 2FP2
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Secreted Chorismate Mutase from Mycobacterium tuberculosis
OverviewOverview
The presence of exported chorismate mutases produced by certain organisms such as Mycobacterium tuberculosis has been shown to correlate with their pathogenicity. As such, these proteins comprise a new group of promising selective drug targets. Here, we report the high-resolution crystal structure of the secreted dimeric chorismate mutase from M. tuberculosis (*MtCM; encoded by Rv1885c), which represents the first 3D-structure of a member of this chorismate mutase family, termed the AroQ(gamma) subclass. Structures are presented both for the unliganded enzyme and for a complex with a transition state analog. The protomer fold resembles the structurally characterized (dimeric) Escherichia coli chorismate mutase domain, but exhibits a new topology, with helix H4 of *MtCM carrying the catalytic site residue missing in the shortened helix H1. Furthermore, the structure of each *MtCM protomer is significantly more compact and only harbors one active site pocket, which is formed entirely by one polypeptide chain. Apart from the structural model, we present evidence as to how the substrate may enter the active site.
About this StructureAbout this Structure
2FP1 is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
ReferenceReference
1.6 A crystal structure of the secreted chorismate mutase from Mycobacterium tuberculosis: novel fold topology revealed., Okvist M, Dey R, Sasso S, Grahn E, Kast P, Krengel U, J Mol Biol. 2006 Apr 14;357(5):1483-99. Epub 2006 Feb 6. PMID:16499927
Page seeded by OCA on Mon Mar 31 03:05:49 2008