1f07: Difference between revisions

Line 1:

[[Image:1f07.gif|left|200px]]<br /><applet load="1f07" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1f07.gif|left|200px]]<br /><applet load="1f07" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1f07, resolution 2.00Å" />

'''STRUCTURE OF COENZYME F420 DEPENDENT TETRAHYDROMETHANOPTERIN REDUCTASE FROM METHANOBACTERIUM THERMOAUTOTROPHICUM'''<br />

==Overview==

Coenzyme F(420)-dependent methylenetetrahydromethanopterin reductase (Mer), is an enzyme of the Cl metabolism in methanogenic and sulfate reducing, archaea. It is composed of identical 35-40 kDa subunits and lacks a, prosthetic group. The crystal structure of Mer from Methanopyrus kandleri, (kMer) revealed in one crystal form a dimeric and in another a tetrameric, oligomerisation state and that from Methanobacterium thermoautotrophicum, (tMer) a dimeric state. Each monomer is primarily composed of a TIM-barrel, fold enlarged by three insertion regions. Insertion regions 1 and 2, contribute to intersubunit interactions. Insertion regions 2 and 3, together with the C-terminal end of the TIM-barrel core form a cleft where, the binding sites of coenzyme F(420) and methylene-tetrahydromethanopterin, are postulated. Close to the coenzyme F(420)-binding site lies a rarely, observed non-prolyl cis-peptide bond. It is surprising that Mer is, structurally most similar to a bacterial FMN-dependent luciferase which, contains a non-prolyl cis-peptide bond at the equivalent position. The, structure of Mer is also related to that of NADP-dependent FAD-harbouring, methylenetetrahydrofolate reductase (MetF). However, Mer and MetF do not, show sequence similarities although they bind related substrates and, catalyze an analogous reaction.

Coenzyme F(420)-dependent methylenetetrahydromethanopterin reductase (Mer) is an enzyme of the Cl metabolism in methanogenic and sulfate reducing archaea. It is composed of identical 35-40 kDa subunits and lacks a prosthetic group. The crystal structure of Mer from Methanopyrus kandleri (kMer) revealed in one crystal form a dimeric and in another a tetrameric oligomerisation state and that from Methanobacterium thermoautotrophicum (tMer) a dimeric state. Each monomer is primarily composed of a TIM-barrel fold enlarged by three insertion regions. Insertion regions 1 and 2 contribute to intersubunit interactions. Insertion regions 2 and 3 together with the C-terminal end of the TIM-barrel core form a cleft where the binding sites of coenzyme F(420) and methylene-tetrahydromethanopterin are postulated. Close to the coenzyme F(420)-binding site lies a rarely observed non-prolyl cis-peptide bond. It is surprising that Mer is structurally most similar to a bacterial FMN-dependent luciferase which contains a non-prolyl cis-peptide bond at the equivalent position. The structure of Mer is also related to that of NADP-dependent FAD-harbouring methylenetetrahydrofolate reductase (MetF). However, Mer and MetF do not show sequence similarities although they bind related substrates and catalyze an analogous reaction.

==About this Structure==

1F07 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus] with CL, MPO and MPD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1F07 OCA].

1F07 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus] with <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=MPO:'>MPO</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F07 OCA].

==Reference==

Line 16:

[[Category: Grabarse, W.]]

[[Category: Shima, S.]]

[[Category: Thauer, R.K.]]

[[Category: Thauer, R K.]]

[[Category: Warkentin, E.]]

[[Category: CL]]

Line 25:

[[Category: tim barrel]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 14~~:29:~~25 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:33:26 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1f07.gif|left|200px]]<br /><applet load="1f07" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1f07.gif|left|200px]]<br /><applet load="1f07" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1f07, resolution 2.00&Aring;" />
 '''STRUCTURE OF COENZYME F420 DEPENDENT TETRAHYDROMETHANOPTERIN REDUCTASE FROM METHANOBACTERIUM THERMOAUTOTROPHICUM'''<br />
 ==Overview==
-Coenzyme F(420)-dependent methylenetetrahydromethanopterin reductase (Mer), is an enzyme of the Cl metabolism in methanogenic and sulfate reducing, archaea. It is composed of identical 35-40 kDa subunits and lacks a, prosthetic group. The crystal structure of Mer from Methanopyrus kandleri, (kMer) revealed in one crystal form a dimeric and in another a tetrameric, oligomerisation state and that from Methanobacterium thermoautotrophicum, (tMer) a dimeric state. Each monomer is primarily composed of a TIM-barrel, fold enlarged by three insertion regions. Insertion regions 1 and 2, contribute to intersubunit interactions. Insertion regions 2 and 3, together with the C-terminal end of the TIM-barrel core form a cleft where, the binding sites of coenzyme F(420) and methylene-tetrahydromethanopterin, are postulated. Close to the coenzyme F(420)-binding site lies a rarely, observed non-prolyl cis-peptide bond. It is surprising that Mer is, structurally most similar to a bacterial FMN-dependent luciferase which, contains a non-prolyl cis-peptide bond at the equivalent position. The, structure of Mer is also related to that of NADP-dependent FAD-harbouring, methylenetetrahydrofolate reductase (MetF). However, Mer and MetF do not, show sequence similarities although they bind related substrates and, catalyze an analogous reaction.
+Coenzyme F(420)-dependent methylenetetrahydromethanopterin reductase (Mer) is an enzyme of the Cl metabolism in methanogenic and sulfate reducing archaea. It is composed of identical 35-40 kDa subunits and lacks a prosthetic group. The crystal structure of Mer from Methanopyrus kandleri (kMer) revealed in one crystal form a dimeric and in another a tetrameric oligomerisation state and that from Methanobacterium thermoautotrophicum (tMer) a dimeric state. Each monomer is primarily composed of a TIM-barrel fold enlarged by three insertion regions. Insertion regions 1 and 2 contribute to intersubunit interactions. Insertion regions 2 and 3 together with the C-terminal end of the TIM-barrel core form a cleft where the binding sites of coenzyme F(420) and methylene-tetrahydromethanopterin are postulated. Close to the coenzyme F(420)-binding site lies a rarely observed non-prolyl cis-peptide bond. It is surprising that Mer is structurally most similar to a bacterial FMN-dependent luciferase which contains a non-prolyl cis-peptide bond at the equivalent position. The structure of Mer is also related to that of NADP-dependent FAD-harbouring methylenetetrahydrofolate reductase (MetF). However, Mer and MetF do not show sequence similarities although they bind related substrates and catalyze an analogous reaction.
 ==About this Structure==
-F07 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus] with CL, MPO and MPD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F07 OCA].
+F07 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus] with <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=MPO:'>MPO</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F07 OCA].
 ==Reference==
@@ Line 16: / Line 16: @@
 [[Category: Grabarse, W.]]
 [[Category: Shima, S.]]
-[[Category: Thauer, R.K.]]
+[[Category: Thauer, R K.]]
 [[Category: Warkentin, E.]]
 [[Category: CL]]
@@ Line 25: / Line 25: @@
 [[Category: tim barrel]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:29:25 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:33:26 2008''