2b0j
From Proteopedia
(New page: 200px<br /><applet load="2b0j" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b0j, resolution 1.75Å" /> '''The crystal structur...) |
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| - | [[Image:2b0j.gif|left|200px]]<br /><applet load="2b0j" size=" | + | [[Image:2b0j.gif|left|200px]]<br /><applet load="2b0j" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2b0j, resolution 1.75Å" /> | caption="2b0j, resolution 1.75Å" /> | ||
'''The crystal structure of the apoenzyme of the iron-sulfur-cluster-free hydrogenase (Hmd)'''<br /> | '''The crystal structure of the apoenzyme of the iron-sulfur-cluster-free hydrogenase (Hmd)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The iron-sulphur cluster-free hydrogenase (Hmd, EC 1.12.98.2) from | + | The iron-sulphur cluster-free hydrogenase (Hmd, EC 1.12.98.2) from methanogenic archaea is a novel type of hydrogenase that tightly binds an iron-containing cofactor. The iron is coordinated by two CO molecules, one sulphur and a pyridone derivative, which is linked via a phosphodiester bond to a guanosine base. We report here on the crystal structure of the Hmd apoenzyme from Methanocaldococcus jannaschii at 1.75 A and from Methanopyrus kandleri at 2.4 A resolution. Homodimeric Hmd reveals a unique architecture composed of one central and two identical peripheral globular units. The central unit is composed of the intertwined C-terminal segments of both subunits, forming a novel intersubunit fold. The two peripheral units consist of the N-terminal domain of each subunit. The Rossmann fold-like structure of the N-terminal domain contains a mononucleotide-binding site, which could harbour the GMP moiety of the cofactor. Another binding site for the iron-containing cofactor is most probably Cys176, which is located at the bottom of a deep intersubunit cleft and which has been shown to be essential for enzyme activity. Adjacent to the iron of the cofactor modelled as a ligand to Cys176, an extended U-shaped extra electron density, interpreted as a polyethyleneglycol fragment, suggests a binding site for the substrate methenyltetrahydromethanopterin. |
==About this Structure== | ==About this Structure== | ||
| - | 2B0J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Active as [http://en.wikipedia.org/wiki/5,10-methenyltetrahydromethanopterin_hydrogenase 5,10-methenyltetrahydromethanopterin hydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.12.98.2 1.12.98.2] Full crystallographic information is available from [http:// | + | 2B0J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Active as [http://en.wikipedia.org/wiki/5,10-methenyltetrahydromethanopterin_hydrogenase 5,10-methenyltetrahydromethanopterin hydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.12.98.2 1.12.98.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B0J OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Ermler, U.]] | [[Category: Ermler, U.]] | ||
| - | [[Category: Hagemeier, C | + | [[Category: Hagemeier, C H.]] |
[[Category: Mamat, B.]] | [[Category: Mamat, B.]] | ||
[[Category: Pilak, O.]] | [[Category: Pilak, O.]] | ||
[[Category: Shima, S.]] | [[Category: Shima, S.]] | ||
| - | [[Category: Thauer, R | + | [[Category: Thauer, R K.]] |
[[Category: Vogt, S.]] | [[Category: Vogt, S.]] | ||
[[Category: Vonrhein, C.]] | [[Category: Vonrhein, C.]] | ||
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[[Category: rossmann fold]] | [[Category: rossmann fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:32:54 2008'' |
Revision as of 14:32, 21 February 2008
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The crystal structure of the apoenzyme of the iron-sulfur-cluster-free hydrogenase (Hmd)
Overview
The iron-sulphur cluster-free hydrogenase (Hmd, EC 1.12.98.2) from methanogenic archaea is a novel type of hydrogenase that tightly binds an iron-containing cofactor. The iron is coordinated by two CO molecules, one sulphur and a pyridone derivative, which is linked via a phosphodiester bond to a guanosine base. We report here on the crystal structure of the Hmd apoenzyme from Methanocaldococcus jannaschii at 1.75 A and from Methanopyrus kandleri at 2.4 A resolution. Homodimeric Hmd reveals a unique architecture composed of one central and two identical peripheral globular units. The central unit is composed of the intertwined C-terminal segments of both subunits, forming a novel intersubunit fold. The two peripheral units consist of the N-terminal domain of each subunit. The Rossmann fold-like structure of the N-terminal domain contains a mononucleotide-binding site, which could harbour the GMP moiety of the cofactor. Another binding site for the iron-containing cofactor is most probably Cys176, which is located at the bottom of a deep intersubunit cleft and which has been shown to be essential for enzyme activity. Adjacent to the iron of the cofactor modelled as a ligand to Cys176, an extended U-shaped extra electron density, interpreted as a polyethyleneglycol fragment, suggests a binding site for the substrate methenyltetrahydromethanopterin.
About this Structure
2B0J is a Single protein structure of sequence from Methanocaldococcus jannaschii. Active as 5,10-methenyltetrahydromethanopterin hydrogenase, with EC number 1.12.98.2 Full crystallographic information is available from OCA.
Reference
The crystal structure of the apoenzyme of the iron-sulphur cluster-free hydrogenase., Pilak O, Mamat B, Vogt S, Hagemeier CH, Thauer RK, Shima S, Vonrhein C, Warkentin E, Ermler U, J Mol Biol. 2006 May 5;358(3):798-809. Epub 2006 Mar 2. PMID:16540118
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