Nitrophorin
From Proteopedia
(Difference between revisions)
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The <scene name='77/776390/Cv/2'>NPs structures contain a large component of β-sheet structure</scene> which is unusual for heme-containing proteins<ref>PMID:15598503</ref>. {{Template:ColorKey_Helix}}, {{Template:ColorKey_Strand}}, | The <scene name='77/776390/Cv/2'>NPs structures contain a large component of β-sheet structure</scene> which is unusual for heme-containing proteins<ref>PMID:15598503</ref>. {{Template:ColorKey_Helix}}, {{Template:ColorKey_Strand}}, | ||
| - | {{Template:ColorKey_Loop}}, {{Template:ColorKey_Turn}}. The NO molecule is bound to the ferric heme opposite the His | + | {{Template:ColorKey_Loop}}, {{Template:ColorKey_Turn}}. The <scene name='77/776390/Cv/3'>NO molecule is bound to the ferric heme opposite the His residue interacting with it</scene><ref>PMID:26167269</ref>. |
</StructureSection> | </StructureSection> | ||
== 3D Structures of deaminase == | == 3D Structures of deaminase == | ||
Revision as of 12:22, 5 February 2018
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3D Structures of deaminase
Updated on 05-February-2018
References
- ↑ Andersen JF, Weichsel A, Balfour CA, Champagne DE, Montfort WR. The crystal structure of nitrophorin 4 at 1.5 A resolution: transport of nitric oxide by a lipocalin-based heme protein. Structure. 1998 Oct 15;6(10):1315-27. PMID:9782054
- ↑ Walker FA. Nitric oxide interaction with insect nitrophorins and thoughts on the electron configuration of the {FeNO}6 complex. J Inorg Biochem. 2005 Jan;99(1):216-36. PMID:15598503 doi:http://dx.doi.org/10.1016/j.jinorgbio.2004.10.009
- ↑ Walker FA. Nitric oxide interaction with insect nitrophorins and thoughts on the electron configuration of the {FeNO}6 complex. J Inorg Biochem. 2005 Jan;99(1):216-36. PMID:15598503 doi:http://dx.doi.org/10.1016/j.jinorgbio.2004.10.009
- ↑ Knipp M, Ogata H, Soavi G, Cerullo G, Allegri A, Abbruzzetti S, Bruno S, Viappiani C, Bidon-Chanal A, Luque FJ. Structure and dynamics of the membrane attaching nitric oxide transporter nitrophorin 7. F1000Res. 2015 Feb 13;4:45. doi: 10.12688/f1000research.6060.1. eCollection 2015. PMID:26167269 doi:http://dx.doi.org/10.12688/f1000research.6060.1
