The C-terminal head domain of Burkholderia pseudomallei BpaC has a striking hydrophilic core with an extensive solvent network.
The C-terminal head domain of Burkholderia pseudomallei BpaC has a striking hydrophilic core with an extensive solvent network.
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类鼻疽伯克霍尔德氏菌BpaC的C-末端头部结构域具有显著的亲水性核心和广泛的溶剂网络。
DOI：
10.1111/mmi.14953
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发表时间：
2022-07
影响因子：
3.6
通讯作者：
Goldman, Adrian
中科院分区：
文献类型：
--
作者：
Kiessling, Andreas R.;Harris, Sarah A.;Weimer, Kathleen M.;Wells, Geoffrey;Goldman, Adrian
关键词：
革兰氏阴性病原体如类鼻疽伯克霍尔德氏菌使用三聚体自转运粘附素如BpaC作为其致病性的关键分子。我们的BpaC头部结构域近膜部分的1.4 nm晶体结构表明，该结构域仅由左手平行β-roll重复序列组成。这是解决的最大的此类结构，具有两个独特的特征。首先，核心不是由典型的疏水性Ile和瓦尔组成，而是主要由亲水性Thr和Asn组成，具有两个不同的溶剂通道。其次，将BpaC与所有其他左手平行β-卷结构进行比较，结果表明蛋白质中头部结构域的位置与带电残基的数量和类型相关。在BpaC中，只有带负电荷的残基面对溶剂，这与左手平行β卷“型”蛋白质YadA的主要正表面电荷形成鲜明对比。我们建议扩展这些头部结构域的定义，根据其不寻常的序列、位置和电荷，将BpaC样头部结构域作为一个单独的亚型纳入其中。我们推测，左手平行β-roll结构的功能可能会有所不同，这取决于它们在结构中的位置。高度带负电荷的BpaC C末端头部结构域的结构揭示了左手平行β卷的一种新亚型。这扩展了先前描述的YadA样头部结构域，其主要是N末端和带正电荷的。由于其核心残基的亲水性，我们在左手平行β卷内确定了一个复杂的埋藏溶剂网络，扩展了三聚体自转运蛋白粘附素的结构域。我们推测这种不寻常的电荷在功能上很重要。
Gram‐negative pathogens like Burkholderia pseudomallei use trimeric autotransporter adhesins such as BpaC as key molecules in their pathogenicity. Our 1.4 Å crystal structure of the membrane‐proximal part of the BpaC head domain shows that the domain is exclusively made of left‐handed parallel β‐roll repeats. This, the largest such structure solved, has two unique features. First, the core, rather than being composed of the canonical hydrophobic Ile and Val, is made up primarily of the hydrophilic Thr and Asn, with two different solvent channels. Second, comparing BpaC to all other left‐handed parallel β‐roll structures showed that the position of the head domain in the protein correlates with the number and type of charged residues. In BpaC, only negatively charged residues face the solvent—in stark contrast to the primarily positive surface charge of the left‐handed parallel β‐roll “type” protein, YadA. We propose extending the definitions of these head domains to include the BpaC‐like head domain as a separate subtype, based on its unusual sequence, position, and charge. We speculate that the function of left‐handed parallel β‐roll structures may differ depending on their position in the structure. The structure of the highly negatively charged C‐terminal head domain of BpaC reveals a novel subtype of left‐handed parallel β roll. This expands the previously described YadA‐like head domains, which are primarily N‐terminal and positively charged. We identified an intricate buried solvent network within a left‐handed parallel β roll due to the hydrophilic nature of its core residues, expanding the structural universe of trimeric autotransporter adhesins. We speculate that the unusual charge is functionally important.
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DOI：
10.1107/s090744491003982x
发表时间：
2011-04
期刊：
Acta crystallographica. Section D, Biological crystallography
影响因子：
--
作者：
Evans PR
通讯作者：
Evans PR
影响因子：
14.9
作者：
Blum M;Chang HY;Chuguransky S;Grego T;Kandasaamy S;Mitchell A;Nuka G;Paysan-Lafosse T;Qureshi M;Raj S;Richardson L;Salazar GA;Williams L;Bork P;Bridge A;Gough J;Haft DH;Letunic I;Marchler-Bauer A;Mi H;Natale DA;Necci M;Orengo CA;Pandurangan AP;Rivoire C;Sigrist CJA;Sillitoe I;Thanki N;Thomas PD;Tosatto SCE;Wu CH;Bateman A;Finn RD
通讯作者：
Finn RD
Islandviewer 4：扩展了大规模数据集基因组岛的预测。
影响因子：
14.9
作者：
Bertelli C;Laird MR;Williams KP;Simon Fraser University Research Computing Group;Lau BY;Hoad G;Winsor GL;Brinkman FSL
通讯作者：
Brinkman FSL
影响因子：
4.2
作者：
Lafontaine ER;Balder R;Michel F;Hogan RJ
通讯作者：
Hogan RJ
影响因子：
14.9
作者：
Buchan, Daniel W. A.;Jones, David T.
通讯作者：
Jones, David T.