1mz4: Difference between revisions

New page: left|200px<br /><applet load="1mz4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mz4, resolution 1.80Å" /> '''Crystal Structure of...
 
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[[Image:1mz4.gif|left|200px]]<br /><applet load="1mz4" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1mz4.gif|left|200px]]<br /><applet load="1mz4" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1mz4, resolution 1.80&Aring;" />
caption="1mz4, resolution 1.80&Aring;" />
'''Crystal Structure of Cytochrome c550 from Thermosynechococcus elongatus'''<br />
'''Crystal Structure of Cytochrome c550 from Thermosynechococcus elongatus'''<br />


==Overview==
==Overview==
First, the crystal structure of cytochrome c-550 (the psbV1 gene product), from the thermophilic cyanobacterium Thermosynechococcus elongatus has, been determined to a resolution of 1.8 A. A comparison of the T. elongatus, cytochrome c-550 structure to its counterparts from mesophilic organisms, Synechocystis 6803 and Arthrospira maxima, suggests that increased numbers, of hydrogen bonds may play a role in the structural basis of, thermostability. The cytochrome c-550 in T. elongatus also differs from, that in Synechocystis 6803 and Arthrospira maxima in its lack of, dimerization and the presence of a trigonal planar molecule, possibly, bicarbonate, tightly bound to the heme propionate oxygen atoms., Cytochromes c-550 from T. elongatus, Synechocystis 6803 and Arthrospira, maxima exhibit different EPR spectra. A correlation has been done between, the heme-axial ligands geometries and the rhombicity calculated from the, EPR spectra. This correlation indicates that binding of cytochrome c-550, to Photosystem II is accompanied by structural changes in the heme, vicinity. Second, the psbV2 gene product has been found and purified. The, UV-visible, EPR and Raman spectra are reported. From the spectroscopic, data and from a theoretical structural model based on the cytochrome c-550, structure it is proposed that the 6th ligand of the heme-iron is the, Tyr86.
First, the crystal structure of cytochrome c-550 (the psbV1 gene product) from the thermophilic cyanobacterium Thermosynechococcus elongatus has been determined to a resolution of 1.8 A. A comparison of the T. elongatus cytochrome c-550 structure to its counterparts from mesophilic organisms, Synechocystis 6803 and Arthrospira maxima, suggests that increased numbers of hydrogen bonds may play a role in the structural basis of thermostability. The cytochrome c-550 in T. elongatus also differs from that in Synechocystis 6803 and Arthrospira maxima in its lack of dimerization and the presence of a trigonal planar molecule, possibly bicarbonate, tightly bound to the heme propionate oxygen atoms. Cytochromes c-550 from T. elongatus, Synechocystis 6803 and Arthrospira maxima exhibit different EPR spectra. A correlation has been done between the heme-axial ligands geometries and the rhombicity calculated from the EPR spectra. This correlation indicates that binding of cytochrome c-550 to Photosystem II is accompanied by structural changes in the heme vicinity. Second, the psbV2 gene product has been found and purified. The UV-visible, EPR and Raman spectra are reported. From the spectroscopic data and from a theoretical structural model based on the cytochrome c-550 structure it is proposed that the 6th ligand of the heme-iron is the Tyr86.


==About this Structure==
==About this Structure==
1MZ4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermosynechococcus_elongatus Thermosynechococcus elongatus] with PO4, BCT, HEM and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MZ4 OCA].  
1MZ4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermosynechococcus_elongatus Thermosynechococcus elongatus] with <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=BCT:'>BCT</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MZ4 OCA].  


==Reference==
==Reference==
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[[Category: Bottin, H.]]
[[Category: Bottin, H.]]
[[Category: Boussac, A.]]
[[Category: Boussac, A.]]
[[Category: Kerfeld, C.A.]]
[[Category: Kerfeld, C A.]]
[[Category: Kirilovsky, D.]]
[[Category: Kirilovsky, D.]]
[[Category: Krogmann, D.]]
[[Category: Krogmann, D.]]
[[Category: Sawaya, M.R.]]
[[Category: Sawaya, M R.]]
[[Category: Sugiura, M.]]
[[Category: Sugiura, M.]]
[[Category: Tran, K.T.]]
[[Category: Tran, K T.]]
[[Category: Yeates, T.O.]]
[[Category: Yeates, T O.]]
[[Category: BCT]]
[[Category: BCT]]
[[Category: GOL]]
[[Category: GOL]]
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[[Category: psii associated cytochrome]]
[[Category: psii associated cytochrome]]


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