Journal:Acta Cryst F:S2053230X19007192

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<StructureSection load='' size='450' side='right' scene='underdevelopment' caption=''>
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<StructureSection load='' size='450' side='right' scene='81/815962/Cv/5' caption=''>
===Crystal Structure of Flavin Dependent Thymidylate Synthase, Thy1, from ''Thermus thermophilus'' having an Extra C Terminal Domain===
===Crystal Structure of Flavin Dependent Thymidylate Synthase, Thy1, from ''Thermus thermophilus'' having an Extra C Terminal Domain===
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<big>Professor Gota Kawai</big> <ref>doi 10.1107/S2053230X19007192</ref>
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<big>A. Ogawa, G. Sampei and G. Kawai</big> <ref>doi 10.1107/S2053230X19007192</ref>
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<hr/>
<b>Molecular Tour</b><br>
<b>Molecular Tour</b><br>
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Thy1 is an enzyme which catalyze the reaction to produce thymidine monophosphate from deoxyuridine monophosphate. We found that Thy1 from Thermus thermophiles, TtThy1, have an extra domain with 48 amino acids at the C terminal. BLAST search showed that the CTD domain exists only for Thy1 from Thermus, Marinithermus, Oceanithermus and Truepera.
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Thy1 is an enzyme which catalyze the reaction to produce thymidine monophosphate from deoxyuridine monophosphate. The Thy1 from ''Thermus thermophilus'' was found , ''Tt''Thy1, have an extra domain with 48 amino acids at the C terminal. BLAST search showed that the CTD domain exists only for Thy1 from Thermus, Marinithermus, Oceanithermus and Truepera. The structure of ''Tt''Thy1 was determined by X-ray crystallography. <scene name='81/815962/Cv/4'>Overall structure</scene> is similar to the known structures and the <scene name='81/815962/Cv/6'>CTD was found to consist of 3 alpha-helices and a beta-strand</scene> ({{Template:ColorKey_Helix}},
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The structure of TtThy1 was determined by X-ray crystallography. Overall structure is similar to the known structures and the CTD was found to consist of 3 alpha-helices and a beta-strand.
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{{Template:ColorKey_Strand}},
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{{Template:ColorKey_Loop}},
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{{Template:ColorKey_Turn}}). <scene name='81/815962/Cv/9'>Structure of CTD</scene>. Conserved residues are in red.
<b>References</b><br>
<b>References</b><br>

Current revision

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