| Structural highlights
5jj8 is a 2 chain structure with sequence from "bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | |
| Gene: | can_1, can, yadF, AO943_21535, AO946_10560, AOD73_25440, AOU28_24465, AOY09_00950, APT60_24635, ATC05_14980, AU380_02155, ERS445055_04974, HV95_21180, HV96_01220, HV97_23895, HV98_01810, HV99_02890, HW00_06825, HW01_20790, HW02_08065, HW03_11820, HW04_25045, HW05_22660, HW06_00905, HW07_08265, HW08_30020, HW09_16360, HW10_17975, IOMTU133_5488, PA257_5879, PA8380_53220, PAERUG_E15_London_28_01_14_01862, PAERUG_P32_London_17_VIM_2_10_11_05532, PAO1OR4768 ("Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885) |
| Activity: | Carbonate dehydratase, with EC number 4.2.1.1 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[A0A072ZBL6_PSEAI] Reversible hydration of carbon dioxide.[RuleBase:RU003956]
Publication Abstract from PubMed
Cryoannealing has been demonstrated to improve the diffraction quality and resolution of crystals of the beta-carbonic anhydrase psCA3 concomitant with a change in space group. After initial flash-cooling in a liquid-nitrogen cryostream an X-ray diffraction data set from a psCA3 crystal was indexed in space group P21212 and was scaled to 2.6 A resolution, but subsequent cryoannealing studies revealed induced protein rearrangements in the crystal contacts, which transformed the space group to I222, with a corresponding improvement of 0.7 A in resolution. Although the change in diffraction resolution was significant, only minor changes in the psCA3 structure, which retained its catalytic `open' conformation, were observed. These findings demonstrate that cryoannealing can be successfully utilized to induce higher diffraction-quality crystals while maintaining enzymatically relevant conformations and may be useful as an experimental tool for structural studies of other enzymes where the initial diffraction quality is poor.
Cryoannealing-induced space-group transition of crystals of the carbonic anhydrase psCA3.,Pinard MA, Kurian JJ, Aggarwal M, Agbandje-McKenna M, McKenna R Acta Crystallogr F Struct Biol Commun. 2016 Jul 1;72(Pt 7):573-7. doi:, 10.1107/S2053230X16009286. Epub 2016 Jun 28. PMID:27380376[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pinard MA, Kurian JJ, Aggarwal M, Agbandje-McKenna M, McKenna R. Cryoannealing-induced space-group transition of crystals of the carbonic anhydrase psCA3. Acta Crystallogr F Struct Biol Commun. 2016 Jul 1;72(Pt 7):573-7. doi:, 10.1107/S2053230X16009286. Epub 2016 Jun 28. PMID:27380376 doi:http://dx.doi.org/10.1107/S2053230X16009286
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