2o0c
From Proteopedia
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|PDB= 2o0c |SIZE=350|CAPTION= <scene name='initialview01'>2o0c</scene>, resolution 2.600Å | |PDB= 2o0c |SIZE=350|CAPTION= <scene name='initialview01'>2o0c</scene>, resolution 2.600Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> | + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NO:NITROGEN+OXIDE'>NO</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= alr2278 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1167 Anabaena sp.]) | |GENE= alr2278 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1167 Anabaena sp.]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2o09|2O09]], [[2o0g|2O0G]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2o0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o0c OCA], [http://www.ebi.ac.uk/pdbsum/2o0c PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2o0c RCSB]</span> | ||
}} | }} | ||
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[[Category: Akker, F van den.]] | [[Category: Akker, F van den.]] | ||
[[Category: Ma, X.]] | [[Category: Ma, X.]] | ||
| - | [[Category: HEM]] | ||
| - | [[Category: NO]] | ||
[[Category: co]] | [[Category: co]] | ||
[[Category: guanylyl cyclase]] | [[Category: guanylyl cyclase]] | ||
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[[Category: no]] | [[Category: no]] | ||
| - | ''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 04:10:55 2008'' |
Revision as of 01:10, 31 March 2008
| |||||||
| , resolution 2.600Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | alr2278 (Anabaena sp.) | ||||||
| Related: | 2O09, 2O0G
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the H-NOX domain from Nostoc sp. PCC 7120 complexed to NO
Overview
Diatomic ligand discrimination by soluble guanylyl cyclase (sGC) is paramount to cardiovascular homeostasis and neuronal signaling. Nitric oxide (NO) stimulates sGC activity 200-fold compared with only four-fold by carbon monoxide (CO). The molecular details of ligand discrimination and differential response to NO and CO are not well understood. These ligands are sensed by the heme domain of sGC, which belongs to the heme nitric oxide oxygen (H-NOX) domain family, also evolutionarily conserved in prokaryotes. Here we report crystal structures of the free, NO-bound, and CO-bound H-NOX domains of a cyanobacterial homolog. These structures and complementary mutational analysis in sGC reveal a molecular ruler mechanism that allows sGC to favor NO over CO while excluding oxygen, concomitant to signaling that exploits differential heme pivoting and heme bending. The heme thereby serves as a flexing wedge, allowing the N-terminal subdomain of H-NOX to shift concurrent with the transition of the six- to five-coordinated NO-bound state upon sGC activation. This transition can be modulated by mutations at sGC residues 74 and 145 and corresponding residues in the cyanobacterial H-NOX homolog.
About this Structure
2O0C is a Single protein structure of sequence from Anabaena sp.. Full crystallographic information is available from OCA.
Reference
NO and CO differentially activate soluble guanylyl cyclase via a heme pivot-bend mechanism., Ma X, Sayed N, Beuve A, van den Akker F, EMBO J. 2007 Jan 24;26(2):578-88. Epub 2007 Jan 11. PMID:17215864
Page seeded by OCA on Mon Mar 31 04:10:55 2008
Categories: Anabaena sp. | Single protein | Akker, F van den. | Ma, X. | Co | Guanylyl cyclase | Heme | No
