|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='4uqf' size='340' side='right'caption='[[4uqf]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='4uqf' size='340' side='right'caption='[[4uqf]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4uqf]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_monocytogenes_hominis"_nyfeldt_1932 "bacterium monocytogenes hominis" nyfeldt 1932]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UQF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UQF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4uqf]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UQF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UQF FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">folE, B4Y57_10615, D3B94_12135, FORC68_1988 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1639 "Bacterium monocytogenes hominis" Nyfeldt 1932])</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]] 2.4Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/GTP_cyclohydrolase_I GTP cyclohydrolase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.16 3.5.4.16] </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=4uqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uqf OCA], [https://pdbe.org/4uqf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uqf RCSB], [https://www.ebi.ac.uk/pdbsum/4uqf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uqf ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4uqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uqf OCA], [http://pdbe.org/4uqf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4uqf RCSB], [http://www.ebi.ac.uk/pdbsum/4uqf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4uqf ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/GCH1_LISMO GCH1_LISMO] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 24: |
Line 25: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacterium monocytogenes hominis nyfeldt 1932]] | |
| - | [[Category: GTP cyclohydrolase I]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Fischer, M]] | + | [[Category: Listeria monocytogenes]] |
| - | [[Category: Graewert, T]] | + | [[Category: Fischer M]] |
| - | [[Category: Perbandt, M]] | + | [[Category: Graewert T]] |
| - | [[Category: Schuessler, S]] | + | [[Category: Perbandt M]] |
| - | [[Category: Allosteric enzyme]]
| + | [[Category: Schuessler S]] |
| - | [[Category: Folic acid biosynthesis]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
GCH1_LISMO
Publication Abstract from PubMed
A putative open reading frame encoding GTP cyclohydrolase I from Listeria monocytogenes was expressed in a recombinant Escherichia coli strain. The recombinant protein was purified and was confirmed to convert GTP to dihydroneopterin triphosphate (Km = 53 microM; vmax = 180 nmol mg(-1) min(-1)). The protein was crystallized from 1.3 M sodium citrate pH 7.3 and the crystal structure was solved at a resolution of 2.4 A (Rfree = 0.226) by molecular replacement using human GTP cyclohydrolase I as a template. The protein is a D5-symmetric decamer with ten topologically equivalent active sites. Screening a small library of about 9000 compounds afforded several inhibitors with IC50 values in the low-micromolar range. Several inhibitors had significant selectivity with regard to human GTP cyclohydrolase I. Hence, GTP cyclohydrolase I may be a potential target for novel drugs directed at microbial infections, including listeriosis, a rare disease with high mortality.
Structure of GTP cyclohydrolase I from Listeria monocytogenes, a potential anti-infective drug target.,Schussler S, Haase I, Perbandt M, Illarionov B, Siemens A, Richter K, Bacher A, Fischer M, Grawert T Acta Crystallogr F Struct Biol Commun. 2019 Sep 1;75(Pt 9):586-592. doi:, 10.1107/S2053230X19010902. Epub 2019 Aug 30. PMID:31475925[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Schussler S, Haase I, Perbandt M, Illarionov B, Siemens A, Richter K, Bacher A, Fischer M, Grawert T. Structure of GTP cyclohydrolase I from Listeria monocytogenes, a potential anti-infective drug target. Acta Crystallogr F Struct Biol Commun. 2019 Sep 1;75(Pt 9):586-592. doi:, 10.1107/S2053230X19010902. Epub 2019 Aug 30. PMID:31475925 doi:http://dx.doi.org/10.1107/S2053230X19010902
|
