On the emergence of P-Loop NTPase and Rossmann enzymes from a Beta-Alpha-Beta ancestral fragment.
P-loop
ancient peptide
enzyme evolution
evolutionary biology
last universal common ancestor
none
protein evolution
Journal
eLife
ISSN: 2050-084X
Titre abrégé: Elife
Pays: England
ID NLM: 101579614
Informations de publication
Date de publication:
09 12 2020
09 12 2020
Historique:
received:
31
10
2020
accepted:
04
12
2020
pubmed:
10
12
2020
medline:
19
3
2021
entrez:
9
12
2020
Statut:
epublish
Résumé
This article is dedicated to the memory of Michael G. Rossmann. Dating back to the last universal common ancestor, P-loop NTPases and Rossmanns comprise the most ubiquitous and diverse enzyme lineages. Despite similarities in their overall architecture and phosphate binding motif, a lack of sequence identity and some fundamental structural differences currently designates them as independent emergences. We systematically searched for structure and sequence elements shared by both lineages. We detected homologous segments that span the first βαβ motif of both lineages, including the phosphate binding loop and a conserved aspartate at the tip of β2. The latter ligates the catalytic metal in P-loop NTPases, while in Rossmanns it binds the nucleotide's ribose moiety. Tubulin, a Rossmann GTPase, demonstrates the potential of the β2-Asp to take either one of these two roles. While convergence cannot be completely ruled out, we show that both lineages likely emerged from a common βαβ segment that comprises the core of these enzyme families to this very day.
Identifiants
pubmed: 33295875
doi: 10.7554/eLife.64415
pii: 64415
pmc: PMC7758060
doi:
pii:
Substances chimiques
AAA Proteins
EC 3.6.4.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Volkswagen Foundation
ID : 94747
Pays : International
Informations de copyright
© 2020, Longo et al.
Déclaration de conflit d'intérêts
LL, JJ, PV, MK, RK, NB, DT No competing interests declared
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