1xb2: Difference between revisions

Line 1:

[[Image:1xb2.gif|left|200px]]<br /><applet load="1xb2" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1xb2.gif|left|200px]]<br /><applet load="1xb2" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1xb2, resolution 2.20Å" />

'''Crystal Structure of Bos taurus mitochondrial Elongation Factor Tu/Ts Complex'''<br />

==Overview==

The three-dimensional structure of the bovine mitochondrial elongation, factor (EF)-Tu.Ts complex (EF-Tumt.Tsmt) has been determined to 2.2-A, resolution using the multi-wavelength anomalous dispersion experimental, method. This complex provides the first insight into the structure of, EF-Tsmt. EF-Tsmt is similar to Escherichia coli and Thermus thermophilus, EF-Ts in the amino-terminal domain. However, the structure of EF-Tsmt, deviates considerably in the core domain with a five-stranded beta-sheet, forming a portion of subdomain N of the core. In E. coli EF-Ts, this, region is composed of a three-stranded sheet. The coiled-coil domain of, the E. coli EF-Ts is largely eroded in EF-Tsmt, in which it consists of a, large loop packed against subdomain C of the core. The conformation of, bovine EF-Tumt in complex with EF-Tsmt is distinct from its conformation, in the EF-Tumt.GDP complex. When domain III of bovine EF-Tumt.GDP is, superimposed on domain III of EF-Tumt in the EF-Tumt.Tsmt complex, helix B, from domain I is also almost superimposed. However, the rest of domain I, is rotated relative to this helix toward domain II, which itself is, rotated toward domain I relative to domain III. Extensive contacts are, observed between the amino-terminal domain of EF-Tsmt and domain I of, EF-Tumt. Furthermore, the conserved TDFV sequence of EF-Tsmt also contacts, domain I with the side chain of Asp139 contacting helix B of EF-Tumt and, inserting the side chain of Phe140 between helices B and C. The structure, of the EF-Tumt.Tsmt complex provides new insights into the nucleotide, exchange mechanism and provides a framework for explaining much of the, mutational data obtained for this complex.

The three-dimensional structure of the bovine mitochondrial elongation factor (EF)-Tu.Ts complex (EF-Tumt.Tsmt) has been determined to 2.2-A resolution using the multi-wavelength anomalous dispersion experimental method. This complex provides the first insight into the structure of EF-Tsmt. EF-Tsmt is similar to Escherichia coli and Thermus thermophilus EF-Ts in the amino-terminal domain. However, the structure of EF-Tsmt deviates considerably in the core domain with a five-stranded beta-sheet forming a portion of subdomain N of the core. In E. coli EF-Ts, this region is composed of a three-stranded sheet. The coiled-coil domain of the E. coli EF-Ts is largely eroded in EF-Tsmt, in which it consists of a large loop packed against subdomain C of the core. The conformation of bovine EF-Tumt in complex with EF-Tsmt is distinct from its conformation in the EF-Tumt.GDP complex. When domain III of bovine EF-Tumt.GDP is superimposed on domain III of EF-Tumt in the EF-Tumt.Tsmt complex, helix B from domain I is also almost superimposed. However, the rest of domain I is rotated relative to this helix toward domain II, which itself is rotated toward domain I relative to domain III. Extensive contacts are observed between the amino-terminal domain of EF-Tsmt and domain I of EF-Tumt. Furthermore, the conserved TDFV sequence of EF-Tsmt also contacts domain I with the side chain of Asp139 contacting helix B of EF-Tumt and inserting the side chain of Phe140 between helices B and C. The structure of the EF-Tumt.Tsmt complex provides new insights into the nucleotide exchange mechanism and provides a framework for explaining much of the mutational data obtained for this complex.

==About this Structure==

1XB2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1XB2 OCA].

1XB2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XB2 OCA].

==Reference==

Line 13:

[[Category: Bos taurus]]

[[Category: Protein complex]]

[[Category: Jeppesen, M.G.]]

[[Category: Jeppesen, M G.]]

[[Category: Navratil, T.]]

[[Category: Nyborg, J.]]

[[Category: Spremulli, L.L.]]

[[Category: Spremulli, L L.]]

[[Category: protein-protein complex]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 05:57:~~19 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:52:56 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1xb2.gif|left|200px]]<br /><applet load="1xb2" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1xb2.gif|left|200px]]<br /><applet load="1xb2" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1xb2, resolution 2.20&Aring;" />
 '''Crystal Structure of Bos taurus mitochondrial Elongation Factor Tu/Ts Complex'''<br />
 ==Overview==
-The three-dimensional structure of the bovine mitochondrial elongation, factor (EF)-Tu.Ts complex (EF-Tumt.Tsmt) has been determined to 2.2-A, resolution using the multi-wavelength anomalous dispersion experimental, method. This complex provides the first insight into the structure of, EF-Tsmt. EF-Tsmt is similar to Escherichia coli and Thermus thermophilus, EF-Ts in the amino-terminal domain. However, the structure of EF-Tsmt, deviates considerably in the core domain with a five-stranded beta-sheet, forming a portion of subdomain N of the core. In E. coli EF-Ts, this, region is composed of a three-stranded sheet. The coiled-coil domain of, the E. coli EF-Ts is largely eroded in EF-Tsmt, in which it consists of a, large loop packed against subdomain C of the core. The conformation of, bovine EF-Tumt in complex with EF-Tsmt is distinct from its conformation, in the EF-Tumt.GDP complex. When domain III of bovine EF-Tumt.GDP is, superimposed on domain III of EF-Tumt in the EF-Tumt.Tsmt complex, helix B, from domain I is also almost superimposed. However, the rest of domain I, is rotated relative to this helix toward domain II, which itself is, rotated toward domain I relative to domain III. Extensive contacts are, observed between the amino-terminal domain of EF-Tsmt and domain I of, EF-Tumt. Furthermore, the conserved TDFV sequence of EF-Tsmt also contacts, domain I with the side chain of Asp139 contacting helix B of EF-Tumt and, inserting the side chain of Phe140 between helices B and C. The structure, of the EF-Tumt.Tsmt complex provides new insights into the nucleotide, exchange mechanism and provides a framework for explaining much of the, mutational data obtained for this complex.
+The three-dimensional structure of the bovine mitochondrial elongation factor (EF)-Tu.Ts complex (EF-Tumt.Tsmt) has been determined to 2.2-A resolution using the multi-wavelength anomalous dispersion experimental method. This complex provides the first insight into the structure of EF-Tsmt. EF-Tsmt is similar to Escherichia coli and Thermus thermophilus EF-Ts in the amino-terminal domain. However, the structure of EF-Tsmt deviates considerably in the core domain with a five-stranded beta-sheet forming a portion of subdomain N of the core. In E. coli EF-Ts, this region is composed of a three-stranded sheet. The coiled-coil domain of the E. coli EF-Ts is largely eroded in EF-Tsmt, in which it consists of a large loop packed against subdomain C of the core. The conformation of bovine EF-Tumt in complex with EF-Tsmt is distinct from its conformation in the EF-Tumt.GDP complex. When domain III of bovine EF-Tumt.GDP is superimposed on domain III of EF-Tumt in the EF-Tumt.Tsmt complex, helix B from domain I is also almost superimposed. However, the rest of domain I is rotated relative to this helix toward domain II, which itself is rotated toward domain I relative to domain III. Extensive contacts are observed between the amino-terminal domain of EF-Tsmt and domain I of EF-Tumt. Furthermore, the conserved TDFV sequence of EF-Tsmt also contacts domain I with the side chain of Asp139 contacting helix B of EF-Tumt and inserting the side chain of Phe140 between helices B and C. The structure of the EF-Tumt.Tsmt complex provides new insights into the nucleotide exchange mechanism and provides a framework for explaining much of the mutational data obtained for this complex.
 ==About this Structure==
-XB2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XB2 OCA].
+XB2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XB2 OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Bos taurus]]
 [[Category: Protein complex]]
-[[Category: Jeppesen, M.G.]]
+[[Category: Jeppesen, M G.]]
 [[Category: Navratil, T.]]
 [[Category: Nyborg, J.]]
-[[Category: Spremulli, L.L.]]
+[[Category: Spremulli, L L.]]
 [[Category: protein-protein complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:57:19 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:52:56 2008''