Sökning: L773:0022 2836 OR L773:1089 8638
> Lantbruksvetenskap >
Subunit Interface D...
Subunit Interface Dynamics in Hexadecameric Rubisco
-
- Van Lun, Michiel (författare)
- Swedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Institutionen för molekylärbiologi,Department of Molecular Biology
-
- van der Spoel, David (författare)
- Uppsala universitet,Beräknings- och systembiologi
-
- Andersson, Inger (författare)
- Swedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Institutionen för molekylärbiologi,Department of Molecular Biology
-
(creator_code:org_t)
-
- Elsevier BV, 2011
- 2011
- Engelska.
-
Ingår i: Journal of Molecular Biology. - : Elsevier BV. - 0022-2836 .- 1089-8638. ; 411:5, s. 1083-1098
- Relaterad länk:
-
https://urn.kb.se/re...
-
visa fler...
-
https://doi.org/10.1...
-
https://res.slu.se/i...
-
visa färre...
Abstract
Ämnesord
Stäng
- Ribulose-1,5-bisphosphate (RuBP) carboxylase/oxygenase (Rubisco) plays an important role in the global carbon cycle as a hub for biomass. Rubisco catalyzes not only the carboxylation of RuBP with carbon dioxide but also a competing oxygenation reaction of RuBP with a negative impact on photosynthetic yield. The functional active site is built from two large (L) subunits that form a dimer. The octameric core of four L(2) dimers is held at each end by a cluster of four small (S) subunits, forming a hexadecamer. Each large subunit contacts more than one S subunit. These interactions exploit the dynamic flexibility of Rubisco, which we address in this study. Here, we describe seven different types of interfaces of hexadecameric Rubisco. We have analyzed these interfaces with respect to the size of the interface area and the number of polar interactions, including salt bridges and hydrogen bonds in a variety of Rubisco enzymes from different organisms and different kingdoms of life, including the Rubisco-like proteins. We have also performed molecular dynamics simulations of Rubisco from Chlamydomonas reinhardtii and mutants thereof. From our computational analyses, we propose structural checkpoints of the S subunit to ensure the functionality and/or assembly of the Rubisco holoenzyme. These checkpoints appear to fine-tune the dynamics of the enzyme in a way that could influence enzyme performance.
Ämnesord
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
- LANTBRUKSVETENSKAPER -- Annan lantbruksvetenskap -- Förnyelsebar bioenergi (hsv//swe)
- AGRICULTURAL SCIENCES -- Other Agricultural Sciences -- Renewable Bioenergy Research (hsv//eng)
- LANTBRUKSVETENSKAPER -- Annan lantbruksvetenskap -- Miljö- och naturvårdsvetenskap (hsv//swe)
- AGRICULTURAL SCIENCES -- Other Agricultural Sciences -- Environmental Sciences related to Agriculture and Land-use (hsv//eng)
- LANTBRUKSVETENSKAPER -- Lantbruksvetenskap, skogsbruk och fiske -- Trädgårdsvetenskap/hortikultur (hsv//swe)
- AGRICULTURAL SCIENCES -- Agriculture, Forestry and Fisheries -- Horticulture (hsv//eng)
- LANTBRUKSVETENSKAPER -- Lantbruksvetenskap, skogsbruk och fiske -- Skogsvetenskap (hsv//swe)
- AGRICULTURAL SCIENCES -- Agriculture, Forestry and Fisheries -- Forest Science (hsv//eng)
- LANTBRUKSVETENSKAPER -- Lantbruksvetenskap, skogsbruk och fiske -- Jordbruksvetenskap (hsv//swe)
- AGRICULTURAL SCIENCES -- Agriculture, Forestry and Fisheries -- Agricultural Science (hsv//eng)
Nyckelord
- ribulose-1
- 5-bisphosphate carboxylase/oxygenase
- Rubisco
- subunit interface
- inter-subunit contacts
- molecular dynamics simulations
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
Hitta via bibliotek
Till lärosätets databas