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- EMDB-32212: Oligomeric interactions maintain active-site structure in a non-c... -

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Basic information

Entry
Database: EMDB / ID: EMD-32212
TitleOligomeric interactions maintain active-site structure in a non-cooperative enzyme family
Map data
Sample
  • Complex: Ternary complex of SCR with NADP and ethyl 4-chloroacetoacetate
    • Other: Asymmetric Tetramer of SCR
KeywordsRossman fold / tetramer / tag-free / wild type with NADPH / OXIDOREDUCTASE
Biological speciesCandida parapsilosis (yeast) / Candida parapsilosis
Methodsingle particle reconstruction / cryo EM / Resolution: 4.03 Å
AuthorsLi YH / Zhang RZ / Wang C / Forouhar F / Clarke O / Vorobiev S / Singh S / Montelione G / Szyperski T / Xu Y / Hunt JF
Funding support China, 2 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)2018YFA0900302 China
Ministry of Education (MoE, China)201706790073 China
CitationJournal: EMBO J / Year: 2022
Title: Oligomeric interactions maintain active-site structure in a noncooperative enzyme family.
Authors: Yaohui Li / Rongzhen Zhang / Chi Wang / Farhad Forouhar / Oliver B Clarke / Sergey Vorobiev / Shikha Singh / Gaetano T Montelione / Thomas Szyperski / Yan Xu / John F Hunt /
Abstract: The evolutionary benefit accounting for widespread conservation of oligomeric structures in proteins lacking evidence of intersubunit cooperativity remains unclear. Here, crystal and cryo-EM ...The evolutionary benefit accounting for widespread conservation of oligomeric structures in proteins lacking evidence of intersubunit cooperativity remains unclear. Here, crystal and cryo-EM structures, and enzymological data, demonstrate that a conserved tetramer interface maintains the active-site structure in one such class of proteins, the short-chain dehydrogenase/reductase (SDR) superfamily. Phylogenetic comparisons support a significantly longer polypeptide being required to maintain an equivalent active-site structure in the context of a single subunit. Oligomerization therefore enhances evolutionary fitness by reducing the metabolic cost of enzyme biosynthesis. The large surface area of the structure-stabilizing oligomeric interface yields a synergistic gain in fitness by increasing tolerance to activity-enhancing yet destabilizing mutations. We demonstrate that two paralogous SDR superfamily enzymes with different specificities can form mixed heterotetramers that combine their individual enzymological properties. This suggests that oligomerization can also diversify the functions generated by a given metabolic investment, enhancing the fitness advantage provided by this architectural strategy.
History
DepositionNov 15, 2021-
Header (metadata) releaseApr 6, 2022-
Map releaseApr 6, 2022-
UpdateDec 13, 2023-
Current statusDec 13, 2023Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_32212.png

Downloads & links

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Map

FileDownload / File: emd_32212.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 0.837 Å
Density
Contour LevelBy AUTHOR: 0.1
Minimum - Maximum-0.4602931 - 0.73260355
Average (Standard dev.)0.00009466373 (±0.015097995)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 214.272 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : Ternary complex of SCR with NADP and ethyl 4-chloroacetoacetate

EntireName: Ternary complex of SCR with NADP and ethyl 4-chloroacetoacetate
Components
  • Complex: Ternary complex of SCR with NADP and ethyl 4-chloroacetoacetate
    • Other: Asymmetric Tetramer of SCR

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Supramolecule #1: Ternary complex of SCR with NADP and ethyl 4-chloroacetoacetate

SupramoleculeName: Ternary complex of SCR with NADP and ethyl 4-chloroacetoacetate
type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Candida parapsilosis (yeast)

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Macromolecule #1: Asymmetric Tetramer of SCR

MacromoleculeName: Asymmetric Tetramer of SCR / type: other / ID: 1 / Classification: other
Source (natural)Organism: Candida parapsilosis
SequenceString: S M G E I E S Y C N K E L G P L P T K A P T L S K N V L D L F S L K G K V A S V T G S S G G I G W A V A E A Y A Q A G A D V A I W Y N S H P A D E K A E H L Q K T Y G V H S K ...String:
S M G E I E S Y C N K E L G P L P T K A P T L S K N V L D L F S L K G K V A S V T G S S G G I G W A V A E A Y A Q A G A D V A I W Y N S H P A D E K A E H L Q K T Y G V H S K A Y K C N I S D P K S V E E T I S Q Q E K D F G T I D V F V A N A G V T W T Q G P E I D V D N Y D S W N K I I S V D L N G V Y Y C S H N I G K I F K K N G K G S L I I T S S I S G K I V N I P Q L Q A P Y N T A K A A C T H L A K S L A I E W A P F A R V N T I S P G Y I D T D I T D F A S K D M K A K W W Q L T P L G R E G L T Q E L V G G Y L Y L A S N A S T F T T G S D V V I D G G Y T C P

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration3 mg/mL
BufferpH: 6
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Number grids imaged: 1 / Number real images: 2885 / Average exposure time: 2.5 sec. / Average electron dose: 56.15 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.17 µm / Nominal defocus min: 1.37 µm / Nominal magnification: 105000
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: PDB ENTRY
Final reconstructionResolution.type: BY AUTHOR / Resolution: 4.03 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 83948
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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Atomic model buiding 1

Initial modelPDB ID:

7dlm


Chain - Source name: PDB / Chain - Initial model type: experimental model
RefinementSpace: REAL / Overall B value: 177

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