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首页> 外文期刊>Biochemistry >HMP Binding Protein ThiY and HMP-P Synthase THI5 Are Structural Homologues
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HMP Binding Protein ThiY and HMP-P Synthase THI5 Are Structural Homologues

机译：HMP结合蛋白ThiY和HMP-P合酶THI5是结构同源物

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TheATP-binding cassette transporter systemThiXYZ transportsN-formyl-4-amino-5-(aminomethyl)-n2-methylpyrimidine (FAMP), a thiamin salvage pathway intermediate, into cells. FAMP is then converted ton4-amino-5-(hydroxymethyl)-2-methylpyrimidine (HMP) and recycled into the thiamin biosynthetic pathway. ThiYnis the periplasmic substrate binding protein of the ThiXYZ system and delivers the substrate FAMP to thentransmembrane domain. We report the crystal structure of Bacillus halodurans ThiY with FAMP bound at 2.4 Anresolution determined by single-wavelength anomalous diffraction phasing. The crystal structure reveals that ThiYnbelongs to the group II periplasmic binding protein family. The closest structural homologues of ThiY arenperiplasmic binding proteins involved in alkanesulfonateitrate and bicarbonate transport. ThiY is alsonstructurally homologous to thiamin binding protein (TbpA) and to thiaminase-I. THI5 is responsible for thensynthesis of 4-amino-5-(hydroxymethyl)-2-methylpyrimidine phosphate in the thiamin biosynthetic pathway ofneukaryotes and is approximately 25% identical in sequence with ThiY. A homology model of Saccharomycesncerevisiae THI5 was generated on the basis of the structure of ThiY. Many features of the thiamin pyrimidinenbinding site are shared between ThiY and THI5, suggesting a common ancestor.
机译：ATP结合盒式转运蛋白系统ThiXYZ将硫胺素挽救途径中间体N-甲酰基-4-氨基-5-（氨基甲基）-n2-甲基嘧啶（FAMP）转运到细胞中。然后将FAMP转化为ton4-氨基-5-（羟甲基）-2-甲基嘧啶（HMP），并循环到硫胺素的生物合成途径中。 ThiYnis ThiXYZ系统的周质底物结合蛋白，并将底物FAMP传递至跨膜结构域。我们报告与FAMP绑定在2.4分辨率由单波长异常衍射定相绑定的嗜碱芽孢杆菌ThiY的晶体结构。晶体结构表明，ThiYn属于II组周质结合蛋白家族。 ThiY异质结合蛋白的最接近结构同源物，涉及链烷磺酸盐/硝酸盐和碳酸氢盐的转运。 ThiY在结构上也与硫胺结合蛋白（TbpA）和硫胺酶-I同源。 THI5负责在真核生物的硫胺素生物合成途径中合成4-氨基-5-（羟甲基）-2-甲基嘧啶磷酸，并且与ThiY的序列约有25％相同。基于ThiY的结构，产生了酿酒酵母THI5的同源模型。硫胺嘧啶结合位点的许多特征在ThiY和THI5之间共享，表明是共同祖先。

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  • 来源
    《Biochemistry》 |2010年第41期|p.8929-8936|共8页
  • 作者

    Shridhar Bale Kanagalaghatta R. Rajashankar Kay Perry Tadhg P. Begley and Steven E. Ealick;

  • 作者单位

    Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853,) Northeastern CollaborativeAccess Team, Building 436, Argonne National Laboratory, Argonne, Illinois 60439, and ^Department of Chemistry,Texas A&M University, College Station, Texas 77843;

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