1caa: Difference between revisions

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X-RAY CRYSTAL STRUCTURES OF THE OXIDIZED AND REDUCED FORMS OF THE RUBREDOXIN FROM THE MARINE HYPERTHERMOPHILIC ARCHAEBACTERIUM PYROCOCCUS FURIOSUS

OverviewOverview

The structures of the oxidized and reduced forms of the rubredoxin from the archaebacterium, Pyrococcus furiosus, an organism that grows optimally at 100 degrees C, have been determined by X-ray crystallography to a resolution of 1.8 A. Crystals of this rubredoxin grow in space group P2(1)2(1)2(1) with room temperature cell dimensions a = 34.6 A, b = 35.5 A, and c = 44.4 A. Initial phases were determined by the method of molecular replacement using the oxidized form of the rubredoxin from the mesophilic eubacterium, Clostridium pasteurianum, as a starting model. The oxidized and reduced models of P. furiosus rubredoxin each contain 414 nonhydrogen protein atoms comprising 53 residues. The model of the oxidized form contains 61 solvent H2O oxygen atoms and has been refined with X-PLOR and TNT to a final R = 0.178 with root mean square (rms) deviations from ideality in bond distances and bond angles of 0.014 A and 2.06 degrees, respectively. The model of the reduced form contains 37 solvent H2O oxygen atoms and has been refined to R = 0.193 with rms deviations from ideality in bond lengths of 0.012 A and in bond angles of 1.95 degrees. The overall structure of P. furiosus rubredoxin is similar to the structures of mesophilic rubredoxins, with the exception of a more extensive hydrogen-bonding network in the beta-sheet region and multiple electrostatic interactions (salt bridge, hydrogen bonds) of the Glu 14 side chain with groups on three other residues (the amino-terminal nitrogen of Ala 1; the indole nitrogen of Trp 3; and the amide nitrogen group of Phe 29). The influence of these and other features upon the thermostability of the P. furiosus protein is discussed.

About this StructureAbout this Structure

1CAA is a Single protein structure of sequence from Pyrococcus furiosus with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

X-ray crystal structures of the oxidized and reduced forms of the rubredoxin from the marine hyperthermophilic archaebacterium Pyrococcus furiosus., Day MW, Hsu BT, Joshua-Tor L, Park JB, Zhou ZH, Adams MW, Rees DC, Protein Sci. 1992 Nov;1(11):1494-507. PMID:1303768

Page seeded by OCA on Thu Feb 21 12:04:03 2008

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OCA

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-[[Image:1caa.gif|left|200px]]<br /><applet load="1caa" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1caa.gif|left|200px]]<br /><applet load="1caa" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1caa, resolution 1.8&Aring;" />
 '''X-RAY CRYSTAL STRUCTURES OF THE OXIDIZED AND REDUCED FORMS OF THE RUBREDOXIN FROM THE MARINE HYPERTHERMOPHILIC ARCHAEBACTERIUM PYROCOCCUS FURIOSUS'''<br />
 ==Overview==
-The structures of the oxidized and reduced forms of the rubredoxin from, the archaebacterium, Pyrococcus furiosus, an organism that grows optimally, at 100 degrees C, have been determined by X-ray crystallography to a, resolution of 1.8 A. Crystals of this rubredoxin grow in space group, P2(1)2(1)2(1) with room temperature cell dimensions a = 34.6 A, b = 35.5, A, and c = 44.4 A. Initial phases were determined by the method of, molecular replacement using the oxidized form of the rubredoxin from the, mesophilic eubacterium, Clostridium pasteurianum, as a starting model. The, oxidized and reduced models of P. furiosus rubredoxin each contain 414, nonhydrogen protein atoms comprising 53 residues. The model of the, oxidized form contains 61 solvent H2O oxygen atoms and has been refined, with X-PLOR and TNT to a final R = 0.178 with root mean square (rms), deviations from ideality in bond distances and bond angles of 0.014 A and, 2.06 degrees, respectively. The model of the reduced form contains 37, solvent H2O oxygen atoms and has been refined to R = 0.193 with rms, deviations from ideality in bond lengths of 0.012 A and in bond angles of, 1.95 degrees. The overall structure of P. furiosus rubredoxin is similar, to the structures of mesophilic rubredoxins, with the exception of a more, extensive hydrogen-bonding network in the beta-sheet region and multiple, electrostatic interactions (salt bridge, hydrogen bonds) of the Glu 14, side chain with groups on three other residues (the amino-terminal, nitrogen of Ala 1; the indole nitrogen of Trp 3; and the amide nitrogen, group of Phe 29). The influence of these and other features upon the, thermostability of the P. furiosus protein is discussed.
+The structures of the oxidized and reduced forms of the rubredoxin from the archaebacterium, Pyrococcus furiosus, an organism that grows optimally at 100 degrees C, have been determined by X-ray crystallography to a resolution of 1.8 A. Crystals of this rubredoxin grow in space group P2(1)2(1)2(1) with room temperature cell dimensions a = 34.6 A, b = 35.5 A, and c = 44.4 A. Initial phases were determined by the method of molecular replacement using the oxidized form of the rubredoxin from the mesophilic eubacterium, Clostridium pasteurianum, as a starting model. The oxidized and reduced models of P. furiosus rubredoxin each contain 414 nonhydrogen protein atoms comprising 53 residues. The model of the oxidized form contains 61 solvent H2O oxygen atoms and has been refined with X-PLOR and TNT to a final R = 0.178 with root mean square (rms) deviations from ideality in bond distances and bond angles of 0.014 A and 2.06 degrees, respectively. The model of the reduced form contains 37 solvent H2O oxygen atoms and has been refined to R = 0.193 with rms deviations from ideality in bond lengths of 0.012 A and in bond angles of 1.95 degrees. The overall structure of P. furiosus rubredoxin is similar to the structures of mesophilic rubredoxins, with the exception of a more extensive hydrogen-bonding network in the beta-sheet region and multiple electrostatic interactions (salt bridge, hydrogen bonds) of the Glu 14 side chain with groups on three other residues (the amino-terminal nitrogen of Ala 1; the indole nitrogen of Trp 3; and the amide nitrogen group of Phe 29). The influence of these and other features upon the thermostability of the P. furiosus protein is discussed.
 ==About this Structure==
-CAA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus] with FE as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CAA OCA].
+CAA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus] with <scene name='pdbligand=FE:'>FE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CAA OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Pyrococcus furiosus]]
 [[Category: Single protein]]
-[[Category: Adams, M.W.W.]]
+[[Category: Adams, M W.W.]]
-[[Category: Day, M.W.]]
+[[Category: Day, M W.]]
-[[Category: Hsu, B.T.]]
+[[Category: Hsu, B T.]]
 [[Category: Joshua-Tor, L.]]
-[[Category: Park, J.B.]]
+[[Category: Park, J B.]]
-[[Category: Rees, D.C.]]
+[[Category: Rees, D C.]]
-[[Category: Zhou, Z.H.]]
+[[Category: Zhou, Z H.]]
 [[Category: FE]]
 [[Category: electron transport]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:18:10 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:04:03 2008''