Pfam家族PF06684（DUF1185）首个代表成员的结构揭示了分支酸变位酶折叠的一种新变体，并暗示其在氨基酸代谢中的作用。
Structures of the first representatives of Pfam family PF06684 (DUF1185) reveal a novel variant of the Bacillus chorismate mutase fold and suggest a role in amino-acid metabolism.
作者信息
Bakolitsa Constantina, Kumar Abhinav, Jin Kevin K, McMullan Daniel, Krishna S Sri, Miller Mitchell D, Abdubek Polat, Acosta Claire, Astakhova Tamara, Axelrod Herbert L, Burra Prasad, Carlton Dennis, Chen Connie, Chiu Hsiu Ju, Clayton Thomas, Das Debanu, Deller Marc C, Duan Lian, Elias Ylva, Ellrott Kyle, Ernst Dustin, Farr Carol L, Feuerhelm Julie, Grant Joanna C, Grzechnik Anna, Grzechnik Slawomir K, Han Gye Won, Jaroszewski Lukasz, Johnson Hope A, Klock Heath E, Knuth Mark W, Kozbial Piotr, Marciano David, Morse Andrew T, Murphy Kevin D, Nigoghossian Edward, Nopakun Amanda, Okach Linda, Paulsen Jessica, Puckett Christina, Reyes Ron, Rife Christopher L, Sefcovic Natasha, Tien Henry J, Trame Christine B, Trout Christina V, van den Bedem Henry, Weekes Dana, White Aprilfawn, Xu Qingping, Hodgson Keith O, Wooley John, Elsliger Marc Andre, Deacon Ashley M, Godzik Adam, Lesley Scott A, Wilson Ian A
机构信息
Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, CA, USA.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Oct 1;66(Pt 10):1182-9. doi: 10.1107/S1744309109050647. Epub 2010 Mar 5.
The crystal structures of BB2672 and SPO0826 were determined to resolutions of 1.7 and 2.1 Å by single-wavelength anomalous dispersion and multiple-wavelength anomalous dispersion, respectively, using the semi-automated high-throughput pipeline of the Joint Center for Structural Genomics (JCSG) as part of the NIGMS Protein Structure Initiative (PSI). These proteins are the first structural representatives of the PF06684 (DUF1185) Pfam family. Structural analysis revealed that both structures adopt a variant of the Bacillus chorismate mutase fold (BCM). The biological unit of both proteins is a hexamer and analysis of homologs indicates that the oligomer interface residues are highly conserved. The conformation of the critical regions for oligomerization appears to be dependent on pH or salt concentration, suggesting that this protein might be subject to environmental regulation. Structural similarities to BCM and genome-context analysis suggest a function in amino-acid synthesis.
作为美国国立综合医学科学研究所蛋白质结构计划（PSI）的一部分，利用结构基因组学联合中心（JCSG）的半自动高通量流程，分别通过单波长反常散射和多波长反常散射，测定了BB2672和SPO0826的晶体结构，分辨率分别为1.7 Å和2.1 Å。这些蛋白质是Pfam家族PF06684（DUF1185）的首批结构代表。结构分析表明，这两种结构均采用了分支酸变位酶折叠（BCM）的变体。这两种蛋白质的生物学单位均为六聚体，对同源物的分析表明，寡聚体界面残基高度保守。寡聚化关键区域的构象似乎取决于pH值或盐浓度，这表明该蛋白质可能受环境调控。与BCM的结构相似性和基因组背景分析表明其在氨基酸合成中发挥作用。
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