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==Solution NMR structure of glutamine amido transferase subunit of gaunosine monophosphate synthetase from Methanocaldococcus jannaschii== | |||
<StructureSection load='2lxn' size='340' side='right' caption='[[2lxn]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2lxn]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LXN FirstGlance]. <br> | |||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">guaAA, MJ1575 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243232 Methanocaldococcus jannaschii DSM 2661])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/GMP_synthase_(glutamine-hydrolyzing) GMP synthase (glutamine-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.5.2 6.3.5.2] </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=2lxn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lxn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lxn RCSB], [http://www.ebi.ac.uk/pdbsum/2lxn PDBsum]</span></td></tr> | |||
</table> | |||
<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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Methanocaldococcus jannaschii dsm 2661]] | [[Category: Methanocaldococcus jannaschii dsm 2661]] | ||
[[Category: Ali, R | [[Category: Ali, R]] | ||
[[Category: Balaram, H | [[Category: Balaram, H]] | ||
[[Category: Kumar, S | [[Category: Kumar, S]] | ||
[[Category: Sarma, S P | [[Category: Sarma, S P]] | ||
[[Category: Ammonia channeling]] | [[Category: Ammonia channeling]] | ||
[[Category: De-novo purine nucleotide biosynthesis]] | [[Category: De-novo purine nucleotide biosynthesis]] | ||
Revision as of 14:40, 18 December 2014
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
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. References
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