Insights into Positive and Negative Requirements for Protein-Protein Interactions by Crystallographic Analysis of the beta-Lactamase Inhibitory Proteins BLIP, BLIP-1, and BLP SCIE SCOPUS
DC Field | Value | Language |
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dc.contributor.author | Gretes, Michael | - |
dc.contributor.author | Lim, Daniel C. | - |
dc.contributor.author | de Castro, Liza | - |
dc.contributor.author | Jensen, Susan E. | - |
dc.contributor.author | Kang, Sung Gyun | - |
dc.contributor.author | Lee, Kye Joon | - |
dc.contributor.author | Strynadka, Natalie C. J. | - |
dc.date.accessioned | 2020-04-20T09:40:29Z | - |
dc.date.available | 2020-04-20T09:40:29Z | - |
dc.date.created | 2020-02-04 | - |
dc.date.issued | 2009-06-05 | - |
dc.identifier.issn | 0022-2836 | - |
dc.identifier.uri | https://sciwatch.kiost.ac.kr/handle/2020.kiost/4279 | - |
dc.description.abstract | beta-Lactamase inhibitory protein (BLIP) binds a variety of beta-lactamase enzymes with wide-ranging specificity. Its binding mechanism and interface interactions are a well-established model system for the characterization of protein-protein interactions. Published studies have examined the binding of BLIP to diverse target beta-lactamases (e.g., TEM-1, SME-1, and SHV-1). However, apart from point mutations of amino acid residues, variability oil the inhibitor side of this enzyme-inhibitor interface has remained Unexplored. Thus, we present crystal structures of two likely BLIP relatives: (1) BLIP-T (solved alone and in complex with TEM-1), which has beta-lactamase inhibitory activity very similar to that of BLIP; and (2) beta-lactamase-inhibitory-protein-like protein (BLP) (in two apo forms, including all ultrahigh-resolution structure), which is unable to inhibit any tested beta-lactamase. Despite categorical differences in species of origin and function, BLIP-1 and BLP share nearly identical backbone conformations, even at loop regions differing in BLIP. We describe interacting residues and provide a comparative Structural analysis of the interactions formed at the interface of BLIP-1-TEM-1 versus those formed at the interface of BLIP-TEM-1. Along with initial attempts to functionally characterize BLP, we examine its amino acid residues that structurally correspond to BLIP/BLIP-I binding hotspots to explain its inability to bind and inhibit TEM-1. We conclude that the BLIP family fold is a robust and flexible scaffold that permits the formation of high-affinity protein-protein interactions while remaining highly selective. Comparison of the two naturally Occurring, distinct binding interfaces built upon this scaffold (BLIP and BLIP-I) shows that there is Substantial variation possible in the subnanomolar binding interaction with TEM-1. The corresponding (non-TEM-1-binding) BLP surface shows that numerous favorable backbone-backbone/backbone-side-chain interactions with a protein partner can be negated by the presence of a few, strongly unfavorable interactions, especially electrostatic repulsions. (C) 2009 Elsevier Ltd. All rights reserved. | - |
dc.description.uri | 1 | - |
dc.language | English | - |
dc.publisher | ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD | - |
dc.subject | STREPTOMYCES-CLAVULIGERUS | - |
dc.subject | TRANSITION-STATE | - |
dc.subject | PI INTERACTIONS | - |
dc.subject | BINDING | - |
dc.subject | ASSOCIATION | - |
dc.subject | RESIDUES | - |
dc.subject | TEM-1 | - |
dc.subject | IDENTIFICATION | - |
dc.subject | ARCHITECTURE | - |
dc.subject | RECOGNITION | - |
dc.title | Insights into Positive and Negative Requirements for Protein-Protein Interactions by Crystallographic Analysis of the beta-Lactamase Inhibitory Proteins BLIP, BLIP-1, and BLP | - |
dc.type | Article | - |
dc.citation.endPage | 305 | - |
dc.citation.startPage | 289 | - |
dc.citation.title | JOURNAL OF MOLECULAR BIOLOGY | - |
dc.citation.volume | 389 | - |
dc.citation.number | 2 | - |
dc.contributor.alternativeName | 강성균 | - |
dc.identifier.bibliographicCitation | JOURNAL OF MOLECULAR BIOLOGY, v.389, no.2, pp.289 - 305 | - |
dc.identifier.doi | 10.1016/j.jmb.2009.03.058 | - |
dc.identifier.wosid | 000266733700007 | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.subject.keywordPlus | STREPTOMYCES-CLAVULIGERUS | - |
dc.subject.keywordPlus | TRANSITION-STATE | - |
dc.subject.keywordPlus | PI INTERACTIONS | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordPlus | ASSOCIATION | - |
dc.subject.keywordPlus | RESIDUES | - |
dc.subject.keywordPlus | TEM-1 | - |
dc.subject.keywordPlus | IDENTIFICATION | - |
dc.subject.keywordPlus | ARCHITECTURE | - |
dc.subject.keywordPlus | RECOGNITION | - |
dc.subject.keywordAuthor | protein-protein interactions | - |
dc.subject.keywordAuthor | interaction hotspots | - |
dc.subject.keywordAuthor | interaction specificity | - |
dc.subject.keywordAuthor | beta-lactamase inhibitory proteins | - |
dc.subject.keywordAuthor | crystal structure | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |