Who's your neighbor? Suggesting alternative assemblies of E/F type bilin lyases from crystal lattice analysis

Maayan Suissa-Szlejf; Jenia Sklyar; Noam Adir

doi:10.1016/j.str.2022.03.015

Who's your neighbor? Suggesting alternative assemblies of E/F type bilin lyases from crystal lattice analysis

Maayan Suissa-Szlejf, Jenia Sklyar, Noam Adir

Chemistry

Technion - Israel Institute of Technology

Research output: Contribution to journal › Review article › peer-review

Abstract

Attachment of bilins to phycobiliproteins is performed by dedicated lyases. In this issue of Structure, Kumarapperuma et al., 2022 present the structure of an E/F type lyase-isomerase that identifies the correct biological interface between active domains, suggesting that a previous E/F lyase misidentified the heterodimer structure from the crystal lattice.

Original language	English
Pages (from-to)	534-536
Number of pages	3
Journal	Structure
Volume	30
Issue number	4
DOIs	https://doi.org/10.1016/j.str.2022.03.015
State	Published - 7 Apr 2022

All Science Journal Classification (ASJC) codes

Molecular Biology
Structural Biology

Access to Document

10.1016/j.str.2022.03.015

Cite this

@article{463b1f7f8a5944228e13c5061374c8f0,

title = "Who's your neighbor? Suggesting alternative assemblies of E/F type bilin lyases from crystal lattice analysis",

abstract = "Attachment of bilins to phycobiliproteins is performed by dedicated lyases. In this issue of Structure, Kumarapperuma et al., 2022 present the structure of an E/F type lyase-isomerase that identifies the correct biological interface between active domains, suggesting that a previous E/F lyase misidentified the heterodimer structure from the crystal lattice.",

author = "Maayan Suissa-Szlejf and Jenia Sklyar and Noam Adir",

note = "Publisher Copyright: {\textcopyright} 2022 Elsevier Ltd",

year = "2022",

month = apr,

day = "7",

doi = "10.1016/j.str.2022.03.015",

language = "الإنجليزيّة",

volume = "30",

pages = "534--536",

journal = "Structure",

issn = "0969-2126",

publisher = "Cell Press",

number = "4",

}

TY - JOUR

T1 - Who's your neighbor? Suggesting alternative assemblies of E/F type bilin lyases from crystal lattice analysis

AU - Suissa-Szlejf, Maayan

AU - Sklyar, Jenia

AU - Adir, Noam

PY - 2022/4/7

Y1 - 2022/4/7

N2 - Attachment of bilins to phycobiliproteins is performed by dedicated lyases. In this issue of Structure, Kumarapperuma et al., 2022 present the structure of an E/F type lyase-isomerase that identifies the correct biological interface between active domains, suggesting that a previous E/F lyase misidentified the heterodimer structure from the crystal lattice.

AB - Attachment of bilins to phycobiliproteins is performed by dedicated lyases. In this issue of Structure, Kumarapperuma et al., 2022 present the structure of an E/F type lyase-isomerase that identifies the correct biological interface between active domains, suggesting that a previous E/F lyase misidentified the heterodimer structure from the crystal lattice.

UR - http://www.scopus.com/inward/record.url?scp=85127498511&partnerID=8YFLogxK

U2 - 10.1016/j.str.2022.03.015

DO - 10.1016/j.str.2022.03.015

M3 - مقالة مرجعية

SN - 0969-2126

VL - 30

SP - 534

EP - 536

JO - Structure

JF - Structure

IS - 4

ER -

Who's your neighbor? Suggesting alternative assemblies of E/F type bilin lyases from crystal lattice analysis

Abstract

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Fingerprint

Cite this