4V59

Crystal structure of fatty acid synthase complexed with nadp+ from thermomyces lanuginosus at 3.1 angstrom resolution.

PDB DOI: https://doi.org/10.2210/pdb4V59/pdb
Entry: 4V59 supersedes: 2UVB, 2UVC

Classification: TRANSFERASE
Organism(s): Thermomyces lanuginosus
Mutation(s): No

Deposited: 2007-03-09 Released: 2014-07-09
Deposition Author(s): Jenni, S., Leibundgut, M., Boehringer, D., Frick, C., Mikolasek, B., Ban, N.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 3.10 Å
R-Value Free: 0.300
R-Value Work: 0.270

wwPDB Validation 3D Report Full Report

Ligand Structure Quality Assessment

This is version 1.3 of the entry. See complete history.

Literature

Structure of Fungal Fatty Acid Synthase and Implications for Iterative Substrate Shuttling

Jenni, S., Leibundgut, M., Boehringer, D., Frick, C., Mikolasek, B., Ban, N.

(2007) Science 316: 254

PubMed: 17431175 Search on PubMed
DOI: https://doi.org/10.1126/science.1138248
Primary Citation of Related Structures:
4V58, 4V59

PubMed Abstract:
We report crystal structures of the 2.6-megadalton alpha6beta6 heterododecameric fatty acid synthase from Thermomyces lanuginosus at 3.1 angstrom resolution. The alpha and beta polypeptide chains form the six catalytic domains required for fatty acid synthesis and numerous expansion segments responsible for extensive intersubunit connections. Detailed views of all active sites provide insights into substrate specificities and catalytic mechanisms and reveal their unique characteristics, which are due to the integration into the multienzyme. The mode of acyl carrier protein attachment in the reaction chamber, together with the spatial distribution of active sites, suggests that iterative substrate shuttling is achieved by a relatively restricted circular motion of the carrier domain in the multifunctional enzyme.

Organizational Affiliation

Institute of Molecular Biology and Biophysics, ETH Zurich, 8092 Zurich, Switzerland.

Macromolecule Content

Total Structure Weight: 2,632.55 kDa
Atom Count: 167,247
Modelled Residue Count: 21,127
Deposited Residue Count: 23,628
Unique protein chains: 2

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
FATTY ACID SYNTHASE ALPHA SUBUNITS	A, B, C, D, E A, B, C, D, E, F	1,878	Thermomyces lanuginosus	Mutation(s): 0
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations Expand
Reference Sequence

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(by identity cutoff) | 3D Structure

Entity ID: 2
Molecule	Chains	Sequence Length	Organism	Details	Image
FATTY ACID SYNTHASE BETA SUBUNITS	G, H, I, J, K G, H, I, J, K, L	2,060	Thermomyces lanuginosus	Mutation(s): 0
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 2 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
NAP Query on NAP Download Ideal Coordinates CCD File SDF format, chain BA [auth K] SDF format, chain DA [auth L] SDF format, chain M [auth A] SDF format, chain N [auth B] SDF format, chain O [auth C] SDF format, chain P [auth D] SDF format, chain Q [auth E] SDF format, chain R [auth F] SDF format, chain T [auth G] SDF format, chain V [auth H] SDF format, chain X [auth I] SDF format, chain Z [auth J] MOL2 format, chain BA [auth K] MOL2 format, chain DA [auth L] MOL2 format, chain M [auth A] MOL2 format, chain N [auth B] MOL2 format, chain O [auth C] MOL2 format, chain P [auth D] MOL2 format, chain Q [auth E] MOL2 format, chain R [auth F] MOL2 format, chain T [auth G] MOL2 format, chain V [auth H] MOL2 format, chain X [auth I] MOL2 format, chain Z [auth J] mmCIF format, chain BA [auth K] mmCIF format, chain DA [auth L] mmCIF format, chain M [auth A] mmCIF format, chain N [auth B] mmCIF format, chain O [auth C] mmCIF format, chain P [auth D] mmCIF format, chain Q [auth E] mmCIF format, chain R [auth F] mmCIF format, chain T [auth G] mmCIF format, chain V [auth H] mmCIF format, chain X [auth I] mmCIF format, chain Z [auth J]	BA [auth K] DA [auth L] M [auth A] N [auth B] O [auth C] BA [auth K], DA [auth L], M [auth A], N [auth B], O [auth C], P [auth D], Q [auth E], R [auth F], T [auth G], V [auth H], X [auth I], Z [auth J]	NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE C₂₁ H₂₈ N₇ O₁₇ P₃ XJLXINKUBYWONI-NNYOXOHSSA-N		Interactions Focus chain BA [auth K] Focus chain DA [auth L] Focus chain M [auth A] Focus chain N [auth B] Focus chain O [auth C] Focus chain P [auth D] Focus chain Q [auth E] Focus chain R [auth F] Focus chain T [auth G] Focus chain V [auth H] Focus chain X [auth I] Focus chain Z [auth J] Interactions & Density Focus chain BA [auth K] Focus chain DA [auth L] Focus chain M [auth A] Focus chain N [auth B] Focus chain O [auth C] Focus chain P [auth D] Focus chain Q [auth E] Focus chain R [auth F] Focus chain T [auth G] Focus chain V [auth H] Focus chain X [auth I] Focus chain Z [auth J]
FMN Query on FMN Download Ideal Coordinates CCD File SDF format, chain AA [auth K] SDF format, chain CA [auth L] SDF format, chain S [auth G] SDF format, chain U [auth H] SDF format, chain W [auth I] SDF format, chain Y [auth J] MOL2 format, chain AA [auth K] MOL2 format, chain CA [auth L] MOL2 format, chain S [auth G] MOL2 format, chain U [auth H] MOL2 format, chain W [auth I] MOL2 format, chain Y [auth J] mmCIF format, chain AA [auth K] mmCIF format, chain CA [auth L] mmCIF format, chain S [auth G] mmCIF format, chain U [auth H] mmCIF format, chain W [auth I] mmCIF format, chain Y [auth J]	AA [auth K] CA [auth L] S [auth G] U [auth H] W [auth I] AA [auth K], CA [auth L], S [auth G], U [auth H], W [auth I], Y [auth J]	FLAVIN MONONUCLEOTIDE C₁₇ H₂₁ N₄ O₉ P FVTCRASFADXXNN-SCRDCRAPSA-N		Interactions Focus chain AA [auth K] Focus chain CA [auth L] Focus chain S [auth G] Focus chain U [auth H] Focus chain W [auth I] Focus chain Y [auth J] Interactions & Density Focus chain AA [auth K] Focus chain CA [auth L] Focus chain S [auth G] Focus chain U [auth H] Focus chain W [auth I] Focus chain Y [auth J]