1x9a: Difference between revisions

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[[Image:1x9a.jpg|left|200px]]<br /><applet load="1x9a" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1x9a.jpg|left|200px]]<br /><applet load="1x9a" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1x9a" />

'''Solution NMR Structure of Protein Tm0979 from Thermotoga maritima. Ontario Center for Structural Proteomics Target TM0979_1_87; Northeast Structural Genomics Consortium Target VT98.'''<br />

==Overview==

We report herein the NMR structure of Tm0979, a structural proteomics, target from Thermotoga maritima. The Tm0979 fold consists of four, beta/alpha units, which form a central parallel beta-sheet with strand, order 1234. The first three helices pack toward one face of the sheet and, the fourth helix packs against the other face. The protein forms a dimer, by adjacent parallel packing of the fourth helices sandwiched between the, two beta-sheets. This fold is very interesting from several points of, view. First, it represents the first structure determination for the DsrH, family of conserved hypothetical proteins, which are involved in oxidation, of intracellular sulfur but have no defined molecular function. Based on, structure and sequence analysis, possible functions are discussed. Second, the fold of Tm0979 most closely resembles YchN-like folds; however the, proteins that adopt these folds differ in secondary structural elements, and quaternary structure. Comparison of these proteins provides insight, into possible mechanisms of evolution of quaternary structure through a, simple mechanism of hydrophobicity-changing mutations of one or two, residues. Third, the Tm0979 fold is found to be similar to flavodoxin-like, folds and beta/alpha barrel proteins, and may provide a link between these, very abundant folds and putative ancestral half-barrel proteins.

We report herein the NMR structure of Tm0979, a structural proteomics target from Thermotoga maritima. The Tm0979 fold consists of four beta/alpha units, which form a central parallel beta-sheet with strand order 1234. The first three helices pack toward one face of the sheet and the fourth helix packs against the other face. The protein forms a dimer by adjacent parallel packing of the fourth helices sandwiched between the two beta-sheets. This fold is very interesting from several points of view. First, it represents the first structure determination for the DsrH family of conserved hypothetical proteins, which are involved in oxidation of intracellular sulfur but have no defined molecular function. Based on structure and sequence analysis, possible functions are discussed. Second, the fold of Tm0979 most closely resembles YchN-like folds; however the proteins that adopt these folds differ in secondary structural elements and quaternary structure. Comparison of these proteins provides insight into possible mechanisms of evolution of quaternary structure through a simple mechanism of hydrophobicity-changing mutations of one or two residues. Third, the Tm0979 fold is found to be similar to flavodoxin-like folds and beta/alpha barrel proteins, and may provide a link between these very abundant folds and putative ancestral half-barrel proteins.

==About this Structure==

1X9A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1X9A OCA].

1X9A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X9A OCA].

==Reference==

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[[Category: Single protein]]

[[Category: Thermotoga maritima]]

[[Category: Arrowsmith, C.H.]]

[[Category: Arrowsmith, C H.]]

[[Category: Gaspar, J.A.]]

[[Category: Gaspar, J A.]]

[[Category: Liu, C.]]

[[Category: Meglei, G.]]

[[Category: Meiering, E.M.]]

[[Category: Meiering, E M.]]

[[Category: NESG, Northeast.Structural.Genomics.Consortium.]]

[[Category: NESG, Northeast Structural Genomics Consortium.]]

[[Category: Pineda-Lucena, A.]]

[[Category: Stathopulos, P.B.]]

[[Category: Stathopulos, P B.]]

[[Category: Stephen, R.]]

[[Category: Vassall, K.A.]]

[[Category: Vassall, K A.]]

[[Category: Wu, B.]]

[[Category: Yee, A.]]

Line 35:

[[Category: structural genomics]]

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@@ Line 1: / Line 1: @@
-[[Image:1x9a.jpg|left|200px]]<br /><applet load="1x9a" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1x9a.jpg|left|200px]]<br /><applet load="1x9a" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1x9a" />
 '''Solution NMR Structure of Protein Tm0979 from Thermotoga maritima. Ontario Center for Structural Proteomics Target TM0979_1_87; Northeast Structural Genomics Consortium Target VT98.'''<br />
 ==Overview==
-We report herein the NMR structure of Tm0979, a structural proteomics, target from Thermotoga maritima. The Tm0979 fold consists of four, beta/alpha units, which form a central parallel beta-sheet with strand, order 1234. The first three helices pack toward one face of the sheet and, the fourth helix packs against the other face. The protein forms a dimer, by adjacent parallel packing of the fourth helices sandwiched between the, two beta-sheets. This fold is very interesting from several points of, view. First, it represents the first structure determination for the DsrH, family of conserved hypothetical proteins, which are involved in oxidation, of intracellular sulfur but have no defined molecular function. Based on, structure and sequence analysis, possible functions are discussed. Second, the fold of Tm0979 most closely resembles YchN-like folds; however the, proteins that adopt these folds differ in secondary structural elements, and quaternary structure. Comparison of these proteins provides insight, into possible mechanisms of evolution of quaternary structure through a, simple mechanism of hydrophobicity-changing mutations of one or two, residues. Third, the Tm0979 fold is found to be similar to flavodoxin-like, folds and beta/alpha barrel proteins, and may provide a link between these, very abundant folds and putative ancestral half-barrel proteins.
+We report herein the NMR structure of Tm0979, a structural proteomics target from Thermotoga maritima. The Tm0979 fold consists of four beta/alpha units, which form a central parallel beta-sheet with strand order 1234. The first three helices pack toward one face of the sheet and the fourth helix packs against the other face. The protein forms a dimer by adjacent parallel packing of the fourth helices sandwiched between the two beta-sheets. This fold is very interesting from several points of view. First, it represents the first structure determination for the DsrH family of conserved hypothetical proteins, which are involved in oxidation of intracellular sulfur but have no defined molecular function. Based on structure and sequence analysis, possible functions are discussed. Second, the fold of Tm0979 most closely resembles YchN-like folds; however the proteins that adopt these folds differ in secondary structural elements and quaternary structure. Comparison of these proteins provides insight into possible mechanisms of evolution of quaternary structure through a simple mechanism of hydrophobicity-changing mutations of one or two residues. Third, the Tm0979 fold is found to be similar to flavodoxin-like folds and beta/alpha barrel proteins, and may provide a link between these very abundant folds and putative ancestral half-barrel proteins.
 ==About this Structure==
-X9A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1X9A OCA].
+X9A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X9A OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Single protein]]
 [[Category: Thermotoga maritima]]
-[[Category: Arrowsmith, C.H.]]
+[[Category: Arrowsmith, C H.]]
-[[Category: Gaspar, J.A.]]
+[[Category: Gaspar, J A.]]
 [[Category: Liu, C.]]
 [[Category: Meglei, G.]]
-[[Category: Meiering, E.M.]]
+[[Category: Meiering, E M.]]
-[[Category: NESG, Northeast.Structural.Genomics.Consortium.]]
+[[Category: NESG, Northeast Structural Genomics Consortium.]]
 [[Category: Pineda-Lucena, A.]]
-[[Category: Stathopulos, P.B.]]
+[[Category: Stathopulos, P B.]]
 [[Category: Stephen, R.]]
-[[Category: Vassall, K.A.]]
+[[Category: Vassall, K A.]]
 [[Category: Wu, B.]]
 [[Category: Yee, A.]]
@@ Line 35: / Line 35: @@
 [[Category: structural genomics]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:41:11 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:52:24 2008''