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New page: left|200px<br /><applet load="1ywd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ywd, resolution 1.08Å" /> '''1.08 A Structure of ...
 
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[[Image:1ywd.gif|left|200px]]<br /><applet load="1ywd" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1ywd.gif|left|200px]]<br /><applet load="1ywd" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1ywd, resolution 1.08&Aring;" />
caption="1ywd, resolution 1.08&Aring;" />
'''1.08 A Structure of Ferrous NP4 (aquo complex)'''<br />
'''1.08 A Structure of Ferrous NP4 (aquo complex)'''<br />


==Overview==
==Overview==
Nitrophorin 4 (NP4), a nitric oxide (NO)-transport protein from the, blood-sucking insect Rhodnius prolixus, uses a ferric (Fe3+) heme to, deliver NO to its victims. NO binding to NP4 induces a large, conformational change and complete desolvation of the distal pocket. The, heme is markedly nonplanar, displaying a ruffling distortion postulated to, contribute to stabilization of the ferric iron. Here, we report the, ferrous (Fe2+) complexes of NP4 with NO, CO, and H2O formed after chemical, reduction of the protein and the characterization of these complexes by, absorption spectroscopy, flash photolysis, and ultrahigh-resolution, crystallography (resolutions vary from 0.9 to 1.08 A). The absorption, spectra, both in solution and in the crystal, are typical for, six-coordinated ferrous complexes. Closure and desolvation of the distal, pocket occurs upon binding CO or NO to the iron regardless of the heme, oxidation state, confirming that the conformational change is driven by, distal ligand polarity. The degree of heme ruffling is coupled to the, nature of the ligand and the iron oxidation state in the following order:, (Fe3+)-NO &gt; (Fe2+)-NO &gt; (Fe2+)-CO &gt; (Fe3+)-H2O &gt; (Fe2+)-H2O. The ferrous, coordination geometry is as expected, except for the proximal histidine, bond, which is shorter than typically found in model compounds. These data, are consistent with heme ruffling and coordination geometry serving to, stabilize the ferric state of the nitrophorins, a requirement for their, physiological function. Possible roles for heme distortion and NO bending, in heme protein function are discussed.
Nitrophorin 4 (NP4), a nitric oxide (NO)-transport protein from the blood-sucking insect Rhodnius prolixus, uses a ferric (Fe3+) heme to deliver NO to its victims. NO binding to NP4 induces a large conformational change and complete desolvation of the distal pocket. The heme is markedly nonplanar, displaying a ruffling distortion postulated to contribute to stabilization of the ferric iron. Here, we report the ferrous (Fe2+) complexes of NP4 with NO, CO, and H2O formed after chemical reduction of the protein and the characterization of these complexes by absorption spectroscopy, flash photolysis, and ultrahigh-resolution crystallography (resolutions vary from 0.9 to 1.08 A). The absorption spectra, both in solution and in the crystal, are typical for six-coordinated ferrous complexes. Closure and desolvation of the distal pocket occurs upon binding CO or NO to the iron regardless of the heme oxidation state, confirming that the conformational change is driven by distal ligand polarity. The degree of heme ruffling is coupled to the nature of the ligand and the iron oxidation state in the following order: (Fe3+)-NO &gt; (Fe2+)-NO &gt; (Fe2+)-CO &gt; (Fe3+)-H2O &gt; (Fe2+)-H2O. The ferrous coordination geometry is as expected, except for the proximal histidine bond, which is shorter than typically found in model compounds. These data are consistent with heme ruffling and coordination geometry serving to stabilize the ferric state of the nitrophorins, a requirement for their physiological function. Possible roles for heme distortion and NO bending in heme protein function are discussed.


==About this Structure==
==About this Structure==
1YWD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodnius_prolixus Rhodnius prolixus] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YWD OCA].  
1YWD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodnius_prolixus Rhodnius prolixus] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YWD OCA].  


==Reference==
==Reference==
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[[Category: Rhodnius prolixus]]
[[Category: Rhodnius prolixus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Maes, E.M.]]
[[Category: Maes, E M.]]
[[Category: Montfort, W.R.]]
[[Category: Montfort, W R.]]
[[Category: Roberts, S.A.]]
[[Category: Roberts, S A.]]
[[Category: Weichsel, A.]]
[[Category: Weichsel, A.]]
[[Category: HEM]]
[[Category: HEM]]
[[Category: ferrous heme; lipocalin fold; beta barrel]]
[[Category: ferrous heme; lipocalin fold; beta barrel]]


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