2lxn: Difference between revisions

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'''Unreleased structure'''


The entry 2lxn is ON HOLD  until Paper Publication
==Solution NMR structure of glutamine amido transferase subunit of gaunosine monophosphate synthetase from Methanocaldococcus jannaschii==
<StructureSection load='2lxn' size='340' side='right'caption='[[2lxn]]' scene=''>
== Structural highlights ==
<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='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>
</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;">
== Publication Abstract from PubMed ==
Sequence 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.


Authors: Ali, R., Kumar, S., Balaram, H., Sarma, S.P.
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<ref>PMID:22203461</ref>


Description: Solution NMR structure of glutamine amido transferase subunit of gaunosine monophosphate synthetase from Methanocaldococcus jannaschii
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2lxn" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[GMP synthase|GMP synthase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Methanocaldococcus jannaschii DSM 2661]]
[[Category: Ali R]]
[[Category: Balaram H]]
[[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

2lxn is a 1 chain structure with sequence from Methanocaldococcus jannaschii DSM 2661. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GUAAA_METJA Catalyzes the synthesis of GMP from XMP (By similarity).

Publication Abstract from PubMed

Sequence 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 Also

References

  1. Ali R, Kumar S, Balaram H, Sarma SP. 1H, 13C, 15N assignment and secondary structure determination of glutamine amido transferase subunit of gaunosine monophosphate synthetase from Methanocaldococcus jannaschii. Biomol NMR Assign. 2012 Oct;6(2):193-6. doi: 10.1007/s12104-011-9354-x. Epub 2011, Dec 28. PMID:22203461 doi:10.1007/s12104-011-9354-x
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