2fc2
From Proteopedia
(New page: 200px<br /><applet load="2fc2" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fc2, resolution 2.20Å" /> '''NO-HEME complex in a...) |
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| - | [[Image:2fc2.gif|left|200px]]<br /><applet load="2fc2" size=" | + | [[Image:2fc2.gif|left|200px]]<br /><applet load="2fc2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2fc2, resolution 2.20Å" /> | caption="2fc2, resolution 2.20Å" /> | ||
'''NO-HEME complex in a bacterial nitric oxide synthase. An Fe(III)-NO may cause nitrosation.'''<br /> | '''NO-HEME complex in a bacterial nitric oxide synthase. An Fe(III)-NO may cause nitrosation.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structures of nitrosyl-heme complexes of a prokaryotic nitric | + | The crystal structures of nitrosyl-heme complexes of a prokaryotic nitric oxide synthase (NOS) from Bacillus subtilis (bsNOS) reveal changes in active-site hydrogen bonding in the presence of the intermediate N(omega)-hydroxy-l-arginine (NOHA) compared to the substrate l-arginine (l-Arg). Correlating with a Val-to-Ile residue substitution in the bsNOS heme pocket, the Fe(II)-NO complex with both l-Arg and NOHA is more bent than the Fe(II)-NO, l-Arg complex of mammalian eNOS [Li, H., Raman, C. S., Martasek, P., Masters, B. S. S., and Poulos, T. L. (2001) Biochemistry 40, 5399-5406]. Structures of the Fe(III)-NO complex with NOHA show a nearly linear nitrosyl group, and in one subunit, partial nitrosation of bound NOHA. In the Fe(II)-NO complexes, the protonated NOHA N(omega) atom forms a short hydrogen bond with the heme-coordinated NO nitrogen, but active-site water molecules are out of hydrogen bonding range with the distal NO oxygen. In contrast, the l-Arg guanidinium interacts more weakly and equally with both NO atoms, and an active-site water molecule hydrogen bonds to the distal NO oxygen. This difference in hydrogen bonding to the nitrosyl group by the two substrates indicates that interactions provided by NOHA may preferentially stabilize an electrophilic peroxo-heme intermediate in the second step of NOS catalysis. |
==About this Structure== | ==About this Structure== | ||
| - | 2FC2 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 HEM, NO, HBI and HAR 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:// | + | 2FC2 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=HEM:'>HEM</scene>, <scene name='pdbligand=NO:'>NO</scene>, <scene name='pdbligand=HBI:'>HBI</scene> and <scene name='pdbligand=HAR:'>HAR</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=2FC2 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: HAR]] | [[Category: HAR]] | ||
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[[Category: no-heme complex]] | [[Category: no-heme complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:19:49 2008'' |
Revision as of 15:19, 21 February 2008
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NO-HEME complex in a bacterial nitric oxide synthase. An Fe(III)-NO may cause nitrosation.
Overview
The crystal structures of nitrosyl-heme complexes of a prokaryotic nitric oxide synthase (NOS) from Bacillus subtilis (bsNOS) reveal changes in active-site hydrogen bonding in the presence of the intermediate N(omega)-hydroxy-l-arginine (NOHA) compared to the substrate l-arginine (l-Arg). Correlating with a Val-to-Ile residue substitution in the bsNOS heme pocket, the Fe(II)-NO complex with both l-Arg and NOHA is more bent than the Fe(II)-NO, l-Arg complex of mammalian eNOS [Li, H., Raman, C. S., Martasek, P., Masters, B. S. S., and Poulos, T. L. (2001) Biochemistry 40, 5399-5406]. Structures of the Fe(III)-NO complex with NOHA show a nearly linear nitrosyl group, and in one subunit, partial nitrosation of bound NOHA. In the Fe(II)-NO complexes, the protonated NOHA N(omega) atom forms a short hydrogen bond with the heme-coordinated NO nitrogen, but active-site water molecules are out of hydrogen bonding range with the distal NO oxygen. In contrast, the l-Arg guanidinium interacts more weakly and equally with both NO atoms, and an active-site water molecule hydrogen bonds to the distal NO oxygen. This difference in hydrogen bonding to the nitrosyl group by the two substrates indicates that interactions provided by NOHA may preferentially stabilize an electrophilic peroxo-heme intermediate in the second step of NOS catalysis.
About this Structure
2FC2 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
Nitrosyl-heme structures of Bacillus subtilis nitric oxide synthase have implications for understanding substrate oxidation., Pant K, Crane BR, Biochemistry. 2006 Feb 28;45(8):2537-44. PMID:16489746
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