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| | <StructureSection load='4b4k' size='340' side='right'caption='[[4b4k]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='4b4k' size='340' side='right'caption='[[4b4k]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4b4k]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_cereus_var._anthracis"_(cohn_1872)_smith_et_al._1946 "bacillus cereus var. anthracis" (cohn 1872) smith et al. 1946]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B4K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B4K FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4b4k]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B4K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B4K FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1xmp|1xmp]], [[4ay3|4ay3]], [[4ay4|4ay4]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4b4k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b4k OCA], [https://pdbe.org/4b4k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b4k RCSB], [https://www.ebi.ac.uk/pdbsum/4b4k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b4k ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4b4k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b4k OCA], [https://pdbe.org/4b4k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b4k RCSB], [https://www.ebi.ac.uk/pdbsum/4b4k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b4k ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/Q81ZH8_BACAN Q81ZH8_BACAN]] Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR) (By similarity).[PIRNR:PIRNR001338]
| + | [https://www.uniprot.org/uniprot/A0A6L7HA71_BACAN A0A6L7HA71_BACAN] Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).[HAMAP-Rule:MF_01929][PIRNR:PIRNR001338] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Bacillus anthracis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Abad-Zapatero, C]] | + | [[Category: Abad-Zapatero C]] |
| - | [[Category: Guasch, A]] | + | [[Category: Guasch A]] |
| - | [[Category: Oliete, R]] | + | [[Category: Oliete R]] |
| - | [[Category: Pous, J]] | + | [[Category: Pous J]] |
| - | [[Category: Rodriguez-Puente, S]] | + | [[Category: Rodriguez-Puente S]] |
| - | [[Category: Isomerase]]
| + | |
| Structural highlights
Function
A0A6L7HA71_BACAN Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).[HAMAP-Rule:MF_01929][PIRNR:PIRNR001338]
Publication Abstract from PubMed
The different changes observed in the diffraction patterns of three different crystal forms (hexagonal, trigonal and monoclinic) of PurE (EC 4.1.1.21), an enzyme from the purine-biosynthesis pathway of Bacillus anthracis, upon a wide range of changes in the relative humidity environment of the crystals are documented. In addition, the changes in the unit-cell parameters, volume and bulk solvent in the three different crystal forms were systematically followed. In an attempt to explain the elastic (P6(5)22) and inelastic (P3(1)21) changes in the diffraction pattern, refined structures of the three different crystal forms determined at 100 K are presented, with particular emphasis on the tertiary and quaternary structural differences, crystal packing, intermolecular and intramolecular interactions and solvent structure. The refined structures show that the precipitant salts, solvent structure (both ordered and bulk) and conformation of the C-termini all play a role in creating a unique cement at both the intramolecular and intermolecular contacts of the different crystal forms. It is suggested that it is the combination of polyethylene glycol and the structure of the ordered water molecules (first and second layers) as well as the structure of the bulk solvent that are the critical factors in the plasticity of the hexagonal crystal packing as opposed to the inelastic responses of the lower symmetry forms.
Elastic and inelastic diffraction changes upon variation of the relative humidity environment of PurE crystals.,Oliete R, Pous J, Rodriguez-Puente S, Abad-Zapatero C, Guasch A Acta Crystallogr D Biol Crystallogr. 2013 Feb;69(Pt 2):194-212. doi:, 10.1107/S090744491204454X. Epub 2013 Jan 19. PMID:23385456[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Oliete R, Pous J, Rodriguez-Puente S, Abad-Zapatero C, Guasch A. Elastic and inelastic diffraction changes upon variation of the relative humidity environment of PurE crystals. Acta Crystallogr D Biol Crystallogr. 2013 Feb;69(Pt 2):194-212. doi:, 10.1107/S090744491204454X. Epub 2013 Jan 19. PMID:23385456 doi:http://dx.doi.org/10.1107/S090744491204454X
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