2003年2月
Crystal structure of AlgQ2, a macromolecule (alginate)-binding protein of Sphingomonas sp A1, complexed with an alginate tetrasaccharide at 1.6-A resolution
JOURNAL OF BIOLOGICAL CHEMISTRY
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- 巻
- 278
- 号
- 8
- 開始ページ
- 6552
- 終了ページ
- 6559
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1074/jbc.M209932200
- 出版者・発行元
- AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Sphingomonas sp. A1 possesses a high molecular weight (HMW) alginate uptake system composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HAM alginate from the pit to the ABC transporter is mediated by the periplasmic HAM alginate-binding proteins AlgQ1 and AlgQ2. We determined the crystal structure of AlgQ2 complexed with an alginate tetrasaccharide using an alginate-free (apo) form as a search model and refined it at 1.6-Angstrom resolution. One tetrasaccharide was found between the N and C-terminal domains, which are connected by three extended hinge loops. The tetrasaccharide complex took on a closed domain form, in contrast to the open domain form of the apo form. The tetrasaccharide was bound in the cleft between the domains through van der Waals interactions and the formation of hydrogen bonds. Among the four sugar residues, the nonreducing end residue was located at the bottom of the cleft and exhibited the largest number of interactions with the surrounding amino acid residues, suggesting that AlgQ2 mainly recognizes and binds to the nonreducing part of a HMW alginate and delivers the polymer to the ABC transporter through conformational changes (open and closed forms) of the two domains.
- リンク情報
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- DOI
- https://doi.org/10.1074/jbc.M209932200
- J-GLOBAL
- https://jglobal.jst.go.jp/detail?JGLOBAL_ID=200902245280703570
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/12486124
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000181129400132&DestApp=WOS_CPL
- ID情報
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- DOI : 10.1074/jbc.M209932200
- ISSN : 0021-9258
- J-Global ID : 200902245280703570
- PubMed ID : 12486124
- Web of Science ID : WOS:000181129400132