Evidence map›Paper›PMID 27114542›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Tracking solvent and protein movement during CO2 release in carbonic anhydrase II crystals.

Chae Un Kim, HyoJin Song, Balendu Sankara Avvaru, Sol M Gruner, SangYoun Park, Robert McKenna

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

20 citing papers in PubMed, 39 citations in OpenAlex.

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  16. Activation of β- and γ-carbonic anhydrases from pathogenic bacteria with tripeptides.Journal of enzyme inhibition and medicinal chemistry · 2018
    Article
  17. Carbonic anhydrase II microcrystals suitable for XFEL studies.Acta crystallographica. Section F, Structural biology communications · 2018
    Article
  18. Article
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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

6 authors at 4 institutions in 2 countries.

Chae Un KimCornell High Energy Synchrotron Source, Cornell University, Ithaca, NY 14853; Department of Physics, Ulsan National Institute of Science and Technology, Ulsan 44919, Republic of Korea; cukim@unist.ac.kr psy@ssu.ac.kr rmckenna@ufl.edu.
HyoJin SongSchool of Systems Biomedical Science, Soongsil University, Seoul 06978, Republic of Korea;
Balendu Sankara AvvaruDepartment of Biochemistry and Molecular Biology, College of Medicine, University of Florida, Gainesville, FL 32610;
Sol M GrunerCornell High Energy Synchrotron Source, Cornell University, Ithaca, NY 14853; Department of Physics, Cornell University, Ithaca, NY 14853.
SangYoun ParkSchool of Systems Biomedical Science, Soongsil University, Seoul 06978, Republic of Korea; cukim@unist.ac.kr psy@ssu.ac.kr rmckenna@ufl.edu.
Robert McKennaDepartment of Biochemistry and Molecular Biology, College of Medicine, University of Florida, Gainesville, FL 32610; cukim@unist.ac.kr psy@ssu.ac.kr rmckenna@ufl.edu.
Soongsil University · KRUniversity of Florida · USCornell University · USUlsan National Institute of Science and Technology · KR

Funding

Overall (pp. 40-62)P41GM103485 · NIGMS · CORNELL UNIVERSITY · PI CERIONE, RICHARD A. · 2012 to 2018
$15.5M
CATALYTIC MECHANISM OF CARBONIC ANHYDRASER01GM025154 · NIGMS · UNIVERSITY OF FLORIDA · PI SILVERMAN, DAVID N · 1985 to 2012
$4.5M
NIGMS NIH HHS P41 GM103485NIGMS NIH HHS R01 GM025154
6 · The paper itself

Abstract

Carbonic anhydrases are mostly zinc metalloenzymes that catalyze the reversible hydration/dehydration of CO2/HCO3 (-) Previously, the X-ray crystal structures of CO2-bound holo (zinc-bound) and apo (zinc-free) human carbonic anhydrase IIs (hCA IIs) were captured at high resolution. Here, we present sequential timeframe structures of holo- [T = 0 s (CO2-bound), 50 s, 3 min, 10 min, 25 min, and 1 h] and apo-hCA IIs [T = 0 s, 50 s, 3 min, and 10 min] during the "slow" release of CO2 Two active site waters, WDW (deep water) and WDW' (this study), replace the vacated space created on CO2 release, and another water, WI (intermediate water), is seen to translocate to the proton wire position W1. In addition, on the rim of the active site pocket, a water W2' (this study), in close proximity to residue His64 and W2, gradually exits the active site, whereas His64 concurrently rotates from pointing away ("out") to pointing toward ("in") active site rotameric conformation. This study provides for the first time, to our knowledge, structural "snapshots" of hCA II intermediate states during the formation of the His64-mediated proton wire that is induced as CO2 is released. Comparison of the holo- and apo-hCA II structures shows that the solvent network rearrangements require the presence of the zinc ion.

Indexed as

Carbon DioxideCarbonic AnhydrasesCatalysisCrystallizationDiffusionEnzyme ActivationFreezingMaterials TestingMolecular ConformationMotionSolventsWaterX-Ray DiffractionCarbon DioxideCarbonic AnhydrasesSolventsWatercarbonic anhydrase IICO2 releasehigh-pressure cryocoolingintermediate states

Identifiers

PMID27114542
PMCPMC4868437
OpenAlexW2342690797

What OpenQuestion holds

Textmetadata
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.