The sulfoquinovosyl glycerol binding protein SmoF binds and accommodates plant sulfolipids.

The sulfoquinovosyl glycerol binding protein SmoF binds and accommodates plant sulfolipids.
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DOI:
10.1016/j.crstbi.2022.03.001
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发表时间:
2022
影响因子:
2.8
通讯作者:
Davies GJ
Davies GJ
中科院分区:
其他
文献类型:
--
作者:
Snow AJD;Sharma M;Lingford JP;Zhang Y;Mui JW;Epa R;Goddard-Borger ED;Williams SJ;Davies GJ

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磺基藜麦糖(SQ)是普遍存在的植物巯基藜麦糖二酰基甘油(SQDG)的阴离子头基。SQDG可经过蜕化作用生成磺基喹啉甘油(SQGro),并进一步进行糖苷裂解生成SQ,后者可通过微生物巯基酵解途径代谢。外源性SQDG代谢物通过跨膜转运蛋白进入细菌。最近在根癌农杆菌中发现的磺基糖酵解磺基喹啉单加氧酶(磺基- smo)途径具有一个质周磺基喹啉甘油结合蛋白(SmoF)和一个atp结合盒(ABC)转运体。本文采用x射线晶体学、差示扫描荧光法和等温滴定量热法研究SmoF对SQ糖苷的识别。这项工作表明,除了SQGro, SmoF还可以结合SQ,一种简单的甲基糖苷,甚至是短链SQDG类似物。这些底物的分子识别是通过与sq -头基团的保守相互作用以及与苷元的更多塑性相互作用来实现的。这表明,瘤胃芽胞杆菌的溶质结合蛋白,以及其他硫糖酵解途径的相关SQ结合蛋白,可以为其宿主生物提供直接获取大多数已知由光养生物产生的SQ代谢物的途径。农杆菌的硫溶磺喹诺糖(SQ)途径通过SQ结合蛋白SmoF导入SQ代谢物。动态结构域运动和构象变化允许SmoF结合SQ以及容纳亚脂类。共配合物的晶体结构阐明了SQ和SQ代谢物结合袋和磺酸盐识别残基。假定的溶质结合蛋白和ABC转运机制存在于所有五种已知的硫糖酵解途径中。
Sulfoquinovose (SQ) is the anionic headgroup of the ubiquitous plant sulfolipid, sulfoquinovosyl diacylglycerol (SQDG). SQDG can undergo delipidation to give sulfoquinovosyl glycerol (SQGro) and further glycoside cleavage to give SQ, which can be metabolized through microbial sulfoglycolytic pathways. Exogenous SQDG metabolites are imported into bacteria through membrane spanning transporter proteins. The recently discovered sulfoglycolytic sulfoquinovose monooxygenase (sulfo-SMO) pathway in Agrobacterium tumefaciens features a periplasmic sulfoquinovosyl glycerol binding protein, SmoF, and an ATP-binding cassette (ABC) transporter. Here, we use X-ray crystallography, differential scanning fluorimetry and isothermal titration calorimetry to study SQ glycoside recognition by SmoF. This work reveals that in addition to SQGro, SmoF can also bind SQ, a simple methyl glycoside and even a short-chain SQDG analogue. Molecular recognition of these substrates is achieved through conserved interactions with the SQ-headgroup together with more plastic interactions with the aglycones. This suggests that the solute binding protein of A. tumefaciens, and related SQ-binding proteins from other sulfoglycolytic pathways, can provide their host organisms direct access to most of the SQ metabolites known to be produced by phototrophs. Sulfoglycolytic sulfoquinovose (SQ) pathway in Agrobacterium uses the SQ binding protein SmoF to import SQ metabolites. Dynamic domain movements and conformational changes allow SmoF to bind SQ as well as to accommodate sulfolipids. Crystal structures of co-complexes elucidate the SQ and SQ-metabolite binding pockets and sulfonate recognising residues. Putative solute binding proteins and ABC transporter machinery are present in all five known sulfoglycolysis pathways.
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