2b0j
From Proteopedia
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- | [[Image:2b0j.gif|left|200px]] | + | [[Image:2b0j.gif|left|200px]] |
- | + | ||
- | '''The crystal structure of the apoenzyme of the iron-sulfur-cluster-free hydrogenase (Hmd)''' | + | {{Structure |
+ | |PDB= 2b0j |SIZE=350|CAPTION= <scene name='initialview01'>2b0j</scene>, resolution 1.75Å | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= [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] | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''The crystal structure of the apoenzyme of the iron-sulfur-cluster-free hydrogenase (Hmd)''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 2B0J is a [ | + | 2B0J is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B0J OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16540118 16540118] |
[[Category: 5,10-methenyltetrahydromethanopterin hydrogenase]] | [[Category: 5,10-methenyltetrahydromethanopterin hydrogenase]] | ||
[[Category: Methanocaldococcus jannaschii]] | [[Category: Methanocaldococcus jannaschii]] | ||
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[[Category: rossmann fold]] | [[Category: rossmann fold]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:56:08 2008'' |
Revision as of 13:56, 20 March 2008
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, resolution 1.75Å | |||||||
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Activity: | 5,10-methenyltetrahydromethanopterin hydrogenase, with EC number 1.12.98.2 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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. 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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