2an2

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[[Image:2an2.gif|left|200px]]<br /><applet load="2an2" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2an2.gif|left|200px]]
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caption="2an2, resolution 2.6&Aring;" />
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'''P332G, A333S Double mutant of the Bacillus subtilis Nitric Oxide Synthase'''<br />
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{{Structure
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|PDB= 2an2 |SIZE=350|CAPTION= <scene name='initialview01'>2an2</scene>, resolution 2.6&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ARG:ARGININE'>ARG</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=H4B:5,6,7,8-TETRAHYDROBIOPTERIN'>H4B</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''P332G, A333S Double mutant of the Bacillus subtilis Nitric Oxide Synthase'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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2AN2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AN2 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16126221 16126221]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16126221 16126221]
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Nitric-oxide synthase]]
[[Category: Nitric-oxide synthase]]
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[[Category: double mutant]]
[[Category: double mutant]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:28:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:51:31 2008''

Revision as of 13:51, 20 March 2008

Image:2an2.gif


PDB ID 2an2

Drag the structure with the mouse to rotate
, resolution 2.6Å
Ligands: , and
Activity: Nitric-oxide synthase, with EC number 1.14.13.39
Coordinates: save as pdb, mmCIF, xml



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. 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 Mar 20 15:51:31 2008

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