2an2
From Proteopedia
(New page: 200px<br /><applet load="2an2" size="450" color="white" frame="true" align="right" spinBox="true" caption="2an2, resolution 2.6Å" /> '''P332G, A333S Double m...) |
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| - | [[Image:2an2.gif|left|200px]]<br /><applet load="2an2" size=" | + | [[Image:2an2.gif|left|200px]]<br /><applet load="2an2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2an2, resolution 2.6Å" /> | caption="2an2, resolution 2.6Å" /> | ||
'''P332G, A333S Double mutant of the Bacillus subtilis Nitric Oxide Synthase'''<br /> | '''P332G, A333S Double mutant of the Bacillus subtilis Nitric Oxide Synthase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Cooperativity among ligand binding, subunit association, and protein | + | Cooperativity among ligand binding, subunit association, and protein folding has implications for enzyme regulation as well as protein aggregation events associated with disease. The binding of substrate l-arginine or cofactor tetrahydrobiopterin converts nitric oxide synthases (NOSs) from a "loose dimer", with an exposed active center and higher sensitivity to proteolysis, to a "tight dimer" competent for catalysis. The crystallographic structure of the Bacillus subtilis NOS loose dimer shows an altered association state with severely destabilized subdomains. Ligand binding or heme reduction converts loose dimers to tight dimers in solution and crystals. Mutations at key positions in the dimer interface that distinguish prokaryotic from eukaryotic NOSs affect the propensity to form loose dimers. The loose dimer structure indicates that non-native interactions can mediate subunit association in NOS. |
==About this Structure== | ==About this Structure== | ||
| - | 2AN2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with ARG, HEM and H4B as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nitric-oxide_synthase Nitric-oxide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.39 1.14.13.39] Full crystallographic information is available from [http:// | + | 2AN2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=ARG:'>ARG</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=H4B:'>H4B</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nitric-oxide_synthase Nitric-oxide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.39 1.14.13.39] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AN2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Nitric-oxide synthase]] | [[Category: Nitric-oxide synthase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Crane, B | + | [[Category: Crane, B R.]] |
[[Category: Pant, K.]] | [[Category: Pant, K.]] | ||
[[Category: ARG]] | [[Category: ARG]] | ||
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[[Category: double mutant]] | [[Category: double mutant]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:28:55 2008'' |
Revision as of 14:28, 21 February 2008
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P332G, A333S Double mutant of the Bacillus subtilis Nitric Oxide Synthase
Overview
Cooperativity among ligand binding, subunit association, and protein folding has implications for enzyme regulation as well as protein aggregation events associated with disease. The binding of substrate l-arginine or cofactor tetrahydrobiopterin converts nitric oxide synthases (NOSs) from a "loose dimer", with an exposed active center and higher sensitivity to proteolysis, to a "tight dimer" competent for catalysis. The crystallographic structure of the Bacillus subtilis NOS loose dimer shows an altered association state with severely destabilized subdomains. Ligand binding or heme reduction converts loose dimers to tight dimers in solution and crystals. Mutations at key positions in the dimer interface that distinguish prokaryotic from eukaryotic NOSs affect the propensity to form loose dimers. The loose dimer structure indicates that non-native interactions can mediate subunit association in NOS.
About this Structure
2AN2 is a Single protein structure of sequence from Bacillus subtilis with , and as ligands. Active as Nitric-oxide synthase, with EC number 1.14.13.39 Full crystallographic information is available from OCA.
Reference
Structure of a loose dimer: an intermediate in nitric oxide synthase assembly., Pant K, Crane BR, J Mol Biol. 2005 Sep 30;352(4):932-40. PMID:16126221
Page seeded by OCA on Thu Feb 21 16:28:55 2008
Categories: Bacillus subtilis | Nitric-oxide synthase | Single protein | Crane, B R. | Pant, K. | ARG | H4B | HEM | Double mutant
