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==Solution NMR structure of glutamine amido transferase subunit of gaunosine monophosphate synthetase from Methanocaldococcus jannaschii== | ==Solution NMR structure of glutamine amido transferase subunit of gaunosine monophosphate synthetase from Methanocaldococcus jannaschii== | ||
<StructureSection load='2lxn' size='340' side='right' caption='[[2lxn | <StructureSection load='2lxn' size='340' side='right'caption='[[2lxn]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2lxn]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2lxn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii_DSM_2661 Methanocaldococcus jannaschii DSM 2661]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LXN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LXN FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2lxn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lxn OCA], [https://pdbe.org/2lxn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lxn RCSB], [https://www.ebi.ac.uk/pdbsum/2lxn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lxn ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/GUAAA_METJA GUAAA_METJA] Catalyzes the synthesis of GMP from XMP (By similarity). | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 15: | Line 17: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2lxn" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[GMP synthase|GMP synthase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Methanocaldococcus jannaschii | [[Category: Large Structures]] | ||
[[Category: Ali | [[Category: Methanocaldococcus jannaschii DSM 2661]] | ||
[[Category: Balaram | [[Category: Ali R]] | ||
[[Category: Kumar | [[Category: Balaram H]] | ||
[[Category: Sarma | [[Category: Kumar S]] | ||
[[Category: Sarma SP]] | |||
Latest revision as of 08:55, 15 May 2024
Solution NMR structure of glutamine amido transferase subunit of gaunosine monophosphate synthetase from Methanocaldococcus jannaschiiSolution NMR structure of glutamine amido transferase subunit of gaunosine monophosphate synthetase from Methanocaldococcus jannaschii
Structural highlights
FunctionGUAAA_METJA Catalyzes the synthesis of GMP from XMP (By similarity). Publication Abstract from PubMedSequence specific resonance assignments have been obtained for (1)H, (13)C and (15)N nuclei of the 21 kDa (188 residues long) glutamine amido transferase subunit of guanosine monophosphate synthetase from Methanocaldococcus jannaschii. From an analysis of (1)H and (13)C(alpha), (13)C(beta) secondary chemical shifts, (3) JH(N)H(alpha) scalar coupling constants and sequential, short and medium range (1)H-(1)H NOEs, it was deduced that the glutamine amido transferase subunit has eleven strands and five helices as the major secondary structural elements in its tertiary structure. 1H, 13C, 15N assignment and secondary structure determination of glutamine amido transferase subunit of gaunosine monophosphate synthetase from Methanocaldococcus jannaschii.,Ali R, Kumar S, Balaram H, Sarma SP Biomol NMR Assign. 2012 Oct;6(2):193-6. doi: 10.1007/s12104-011-9354-x. Epub 2011, Dec 28. PMID:22203461[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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