1ftr
From Proteopedia
(New page: 200px<br /><applet load="1ftr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ftr, resolution 1.7Å" /> '''FORMYLMETHANOFURAN:TE...) |
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| - | [[Image:1ftr.jpg|left|200px]]<br /><applet load="1ftr" size=" | + | [[Image:1ftr.jpg|left|200px]]<br /><applet load="1ftr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ftr, resolution 1.7Å" /> | caption="1ftr, resolution 1.7Å" /> | ||
'''FORMYLMETHANOFURAN:TETRAHYDROMETHANOPTERIN FORMYLTRANSFERASE FROM METHANOPYRUS KANDLERI'''<br /> | '''FORMYLMETHANOFURAN:TETRAHYDROMETHANOPTERIN FORMYLTRANSFERASE FROM METHANOPYRUS KANDLERI'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: Formylmethanofuran: tetrahydromethanopterin formyltransferase | + | BACKGROUND: Formylmethanofuran: tetrahydromethanopterin formyltransferase (Ftr) from the methanogenic Archaeon Methanopyrus kandleri (optimum growth temperature 98 degrees C) is a hyperthermophilic enzyme that is absolutely dependent on the presence of lyotropic salts for activity and thermostability. The enzyme is involved in the pathway of carbon dioxide reduction to methane and catalyzes the transfer of formyl from formylmethanofuran to tetrahydromethanopterin. RESULTS: The crystal structure of Ftr, determined to a resolution of 1:73 AE reveals a homotetramer composed essentially of two dimers. Each subunit is subdivided into two tightly associated lobes both consisting of a predominantly antiparallel beta sheet flanked by alpha helices forming an alpha/beta sandwich structure. The approximate location of the active site was detected in a region close to the dimer interface. CONCLUSIONS: The adaptation of Ftr against high lyotropic salt concentrations is structurally reflected by a large number of negatively charged residues and their high local concentration on the surface of the protein. The salt-dependent thermostability of Ftr might be explained on a molecular basis by ionic interactions at the protein surface, involving both protein and inorganic salt ions, and the mainly hydrophobic interactions between the subunits and within the core. |
==About this Structure== | ==About this Structure== | ||
| - | 1FTR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanopyrus_kandleri Methanopyrus kandleri]. Active as [http://en.wikipedia.org/wiki/Formylmethanofuran--tetrahydromethanopterin_N-formyltransferase Formylmethanofuran--tetrahydromethanopterin N-formyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.101 2.3.1.101] Full crystallographic information is available from [http:// | + | 1FTR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanopyrus_kandleri Methanopyrus kandleri]. Active as [http://en.wikipedia.org/wiki/Formylmethanofuran--tetrahydromethanopterin_N-formyltransferase Formylmethanofuran--tetrahydromethanopterin N-formyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.101 2.3.1.101] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FTR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Ermler, U.]] | [[Category: Ermler, U.]] | ||
| - | [[Category: Merckel, M | + | [[Category: Merckel, M C.]] |
[[Category: Shima, S.]] | [[Category: Shima, S.]] | ||
| - | [[Category: Thauer, R | + | [[Category: Thauer, R K.]] |
[[Category: acyltransferase]] | [[Category: acyltransferase]] | ||
[[Category: archae]] | [[Category: archae]] | ||
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[[Category: methanogenesis]] | [[Category: methanogenesis]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:42:33 2008'' |
Revision as of 10:42, 21 February 2008
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FORMYLMETHANOFURAN:TETRAHYDROMETHANOPTERIN FORMYLTRANSFERASE FROM METHANOPYRUS KANDLERI
Overview
BACKGROUND: Formylmethanofuran: tetrahydromethanopterin formyltransferase (Ftr) from the methanogenic Archaeon Methanopyrus kandleri (optimum growth temperature 98 degrees C) is a hyperthermophilic enzyme that is absolutely dependent on the presence of lyotropic salts for activity and thermostability. The enzyme is involved in the pathway of carbon dioxide reduction to methane and catalyzes the transfer of formyl from formylmethanofuran to tetrahydromethanopterin. RESULTS: The crystal structure of Ftr, determined to a resolution of 1:73 AE reveals a homotetramer composed essentially of two dimers. Each subunit is subdivided into two tightly associated lobes both consisting of a predominantly antiparallel beta sheet flanked by alpha helices forming an alpha/beta sandwich structure. The approximate location of the active site was detected in a region close to the dimer interface. CONCLUSIONS: The adaptation of Ftr against high lyotropic salt concentrations is structurally reflected by a large number of negatively charged residues and their high local concentration on the surface of the protein. The salt-dependent thermostability of Ftr might be explained on a molecular basis by ionic interactions at the protein surface, involving both protein and inorganic salt ions, and the mainly hydrophobic interactions between the subunits and within the core.
About this Structure
1FTR is a Single protein structure of sequence from Methanopyrus kandleri. Active as Formylmethanofuran--tetrahydromethanopterin N-formyltransferase, with EC number 2.3.1.101 Full crystallographic information is available from OCA.
Reference
Formylmethanofuran: tetrahydromethanopterin formyltransferase from Methanopyrus kandleri - new insights into salt-dependence and thermostability., Ermler U, Merckel M, Thauer R, Shima S, Structure. 1997 May 15;5(5):635-46. PMID:9195883
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