Evidence map›Paper›PMID 20402538›Full record

ArticleACS chemical biology2010

X-ray structures of isopentenyl phosphate kinase.

Mark F Mabanglo, Heidi L Schubert, Mo Chen, Christopher P Hill, C Dale Poulter

Abstract read
In one paragraph

Article in ACS chemical biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.6field-weighted citation impact, top 17% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. ACS chemical biology · 2022
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Crystallization and preliminary X-ray diffraction analysis of MJ0458, an adenylate kinase from Methanocaldococcus jannaschii.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Enzymes of the mevalonate pathway of isoprenoid biosynthesis.Archives of biochemistry and biophysics · 2011
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Mark F MabangloDepartment of Chemistry, University of Utah, Salt Lake City, 84112, USA.
Heidi L Schubert
Mo Chen
Christopher P Hill
C Dale Poulter
University of Utah · US

Funding

STUDIES OF STEROL BIOSYNTHESISR01GM025521 · NIGMS · UNIVERSITY OF UTAH · PI POULTER, CHARLES DALE · 1985 to 2014
$5.9M
STRUCTURAL STUDIES ON HEME BIOSYNTHETIC ENZYMESR01GM056775 · NIGMS · UNIVERSITY OF UTAH · PI HILL, CHRISTOPHER P. · 1998 to 2009
$2.7M
NIGMS NIH HHS GM 25521NIGMS NIH HHS GM 56775NIGMS NIH HHS R01 GM025521NIGMS NIH HHS R01 GM056775
6 · The paper itself

Abstract

Isoprenoid compounds are ubiquitous in nature, participating in important biological phenomena such as signal transduction, aerobic cellular respiration, photosynthesis, insect communication, and many others. They are derived from the 5-carbon isoprenoid substrates isopentenyl diphosphate (IPP) and its isomer dimethylallyl diphosphate (DMAPP). In Archaea and Eukarya, these building blocks are synthesized via the mevalonate pathway. However, the genes required to convert mevalonate phosphate (MP) to IPP are missing in several species of Archaea. An enzyme with isopentenyl phosphate kinase (IPK) activity was recently discovered in Methanocaldococcus jannaschii (MJ), suggesting a departure from the classical sequence of converting MP to IPP. We have determined the high-resolution crystal structures of isopentenyl phosphate kinases in complex with both substrates and products from Thermoplasma acidophilum (THA), as well as the IPK from Methanothermobacter thermautotrophicus (MTH), by means of single-wavelength anomalous diffraction (SAD) and molecular replacement. A histidine residue (His50) in THA IPK makes a hydrogen bond with the terminal phosphates of IP and IPP, poising these molecules for phosphoryl transfer through an in-line geometry. Moreover, a lysine residue (Lys14) makes hydrogen bonds with nonbridging oxygen atoms at P(alpha) and P(gamma) and with the P(beta)-P(gamma) bridging oxygen atom in ATP. These interactions suggest a transition-state-stabilizing role for this residue. Lys14 is a part of a newly discovered "lysine triangle" catalytic motif in IPKs that also includes Lys5 and Lys205. Moreover, His50, Lys5, Lys14, and Lys205 are conserved in all IPKs and can therefore serve as fingerprints for identifying new homologues.

Indexed as

HemiterpenesMethanobacteriaceaeProtein KinasesThermoplasmaAmino Acid SequenceArchaeal ProteinsBinding SitesBiosynthetic PathwaysCrystallography, X-RayHydrogen BondingModels, MolecularProtein ConformationProtein Structure, SecondaryProtein Structure, TertiarySequence Homology, Amino AcidArchaeal ProteinsHemiterpenesisopentenyl monophosphate kinaseProtein Kinases

Identifiers

PMID20402538
PMCPMC2879073
OpenAlexW2053693038

What OpenQuestion holds

Textmetadata
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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.