Dataset Information

Structure of LP2179, the first representative of Pfam family PF08866, suggests a new fold with a role in amino-acid metabolism.

ABSTRACT: The structure of LP2179, a member of the PF08866 (DUF1831) family, suggests a novel ?+? fold comprising two ?-sheets packed against a single helix. A remote structural similarity to two other uncharacterized protein families specific to the Bacillus genus (PF08868 and PF08968), as well as to prokaryotic S-adenosylmethionine decarboxylases, is consistent with a role in amino-acid metabolism. Genomic neighborhood analysis of LP2179 supports this functional assignment, which might also then be extended to PF08868 and PF08968.

SUBMITTER: Bakolitsa C

PROVIDER: S-EPMC2954206 | biostudies-literature | 2010 Oct

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Structure of LP2179, the first representative of Pfam family PF08866, suggests a new fold with a role in amino-acid metabolism.

Bakolitsa Constantina C Kumar Abhinav A Carlton Dennis D Miller Mitchell D MD Krishna S Sri SS Abdubek Polat P Astakhova Tamara T Axelrod Herbert L HL Chiu Hsiu Ju HJ Clayton Thomas T Deller Marc C MC Duan Lian L Elsliger Marc André MA Feuerhelm Julie J Grzechnik Slawomir K SK Grant Joanna C JC Han Gye Won GW Jaroszewski Lukasz L Jin Kevin K KK Klock Heath E HE Knuth Mark W MW Kozbial Piotr P Marciano David D McMullan Daniel D Morse Andrew T AT Nigoghossian Edward E Okach Linda L Oommachen Silvya S Paulsen Jessica J Reyes Ron R Rife Christopher L CL Tien Henry J HJ Trout Christina V CV van den Bedem Henry H Weekes Dana D Xu Qingping Q Hodgson Keith O KO Wooley John J Deacon Ashley M AM Godzik Adam A Lesley Scott A SA Wilson Ian A IA

Acta crystallographica. Section F, Structural biology and crystallization communications 20091027 Pt 10

The structure of LP2179, a member of the PF08866 (DUF1831) family, suggests a novel α+β fold comprising two β-sheets packed against a single helix. A remote structural similarity to two other uncharacterized protein families specific to the Bacillus genus (PF08868 and PF08968), as well as to prokaryotic S-adenosylmethionine decarboxylases, is consistent with a role in amino-acid metabolism. Genomic neighborhood analysis of LP2179 supports this functional assignment, which might also then be exte ...[more]

PMID: 20944212

Dataset Information

Structure of LP2179, the first representative of Pfam family PF08866, suggests a new fold with a role in amino-acid metabolism.

Publications

Structure of LP2179, the first representative of Pfam family PF08866, suggests a new fold with a role in amino-acid metabolism.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets

Similar Datasets

The structure of the first representative of Pfam family PF06475 reveals a new fold with possible involvement in glycolipid metabolism.
| S-EPMC2954207 | biostudies-literature

Structure of the first representative of Pfam family PF09410 (DUF2006) reveals a structural signature of the calycin superfamily that suggests a role in lipid metabolism.
| S-EPMC2954199 | biostudies-literature

The structure of the first representative of Pfam family PF09836 reveals a two-domain organization and suggests involvement in transcriptional regulation.
| S-EPMC2954202 | biostudies-literature

Structures of the first representatives of Pfam family PF06684 (DUF1185) reveal a novel variant of the Bacillus chorismate mutase fold and suggest a role in amino-acid metabolism.
| S-EPMC2954203 | biostudies-literature

The structure of SSO2064, the first representative of Pfam family PF01796, reveals a novel two-domain zinc-ribbon OB-fold architecture with a potential acyl-CoA-binding role.
| S-EPMC2954200 | biostudies-literature

Solution NMR structure of Alr2454 from Nostoc sp. PCC 7120, the first structural representative of Pfam domain family PF11267.
| S-EPMC3897273 | biostudies-literature

A Novel Subfamily of Bacterial AAT-Fold Basic Amino Acid Decarboxylases and Functional Characterization of Its First Representative: Pseudomonas aeruginosa LdcA.
| S-EPMC6257575 | biostudies-literature

Structures of the first representatives of Pfam family PF06938 (DUF1285) reveal a new fold with repeated structural motifs and possible involvement in signal transduction.
| S-EPMC2954208 | biostudies-literature

Structure of the first representative of Pfam family PF04016 (DUF364) reveals enolase and Rossmann-like folds that combine to form a unique active site with a possible role in heavy-metal chelation.
| S-EPMC2954201 | biostudies-literature

The first structure in a family of peptidase inhibitors reveals an unusual Ig-like fold.
| S-EPMC3901451 | biostudies-literature