Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Homology modeling of Neurospora crassa geranylgeranyl pyrophosphate synthase: structural interpretation of mutant phenotypes.

Protein engineering - 1 Sept 1997

Quondam M, Barbato C, Pickford A, Helmer-Citterich M, Macino G

Abstract excerpt

A model of the tertiary structure of the Neurospora crassa carotenogenic prenyltransferase, geranylgeranyl pyrophosphate synthase (GGPPS), is presented, based on structural homology with other prenyltransferases and on the crystal structure of recombinant avian farnesyl pyrophosphate synthase (FPPS). The conserved aspartate-rich motifs DDxx(xx)D and associated basic residues, considered to be the active sites for...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Molecular Sequence Data

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Mutagenesis, Site-Directed

Share to Phenotype

Share to Point Mutation

Share to Protein Conformation

Share to Recombinant Proteins

Share to Sequence Homology, Amino Acid

Source

Identifiers

PMID: 9464568
DOI: 10.1093/protein/10.9.1047

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Homology modeling of Neurospora crassa geranylgeranyl pyrophosphate synthase: structural interpretation of mutant phenotypes.PMID 9464568Read ↗

Engineering dimer mutants of human geranylgeranyl pyrophosphate synthase.Semantic proximity Read ↗

Mild RIP-an alternative method for in vivo mutagenesis of the albino-3 gene in Neurospora crassa.Semantic proximity Read ↗

Functional characterization of the Xanthophyllomyces dendrorhous farnesyl pyrophosphate synthase and geranylgeranyl pyrophosphate synthase encoding genes that are involved in the synthesis of isoprenoid precursors.Semantic proximity Read ↗

Distinct structural elements dictate the specificity of the type III pentaketide synthase from Neurospora crassa.Semantic proximity Read ↗

Conversion of product specificity of archaebacterial geranylgeranyl-diphosphate synthase. Identification of essential amino acid residues for chain length determination of prenyltransferase reaction.Semantic proximity Read ↗

Directed evolution of Escherichia coli farnesyl diphosphate synthase (IspA) reveals novel structural determinants of chain length specificity.Semantic proximity Read ↗

An alternative mechanism of product chain-length determination in type III geranylgeranyl diphosphate synthase.Semantic proximity Read ↗

Genetic analysis and enzyme activity suggest the existence of more than one minimal functional unit capable of synthesizing phosphoribosyl pyrophosphate in Saccharomyces cerevisiae.Semantic proximity Read ↗

Plant-type phytoene desaturase: Functional evaluation of structural implications.Semantic proximity Read ↗

Structural features conferring dual geranyl/farnesyl diphosphate synthase activity to an aphid prenyltransferase.Semantic proximity Read ↗

Analysis of al-2 mutations in Neurospora.Semantic proximity Read ↗

Substrate specificity determinants in the farnesyltransferase beta-subunit.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.