GMP synthase: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
Human GMPS structure contains <scene name='51/516475/Cv/10'>2 dimerization domains (D1 and D2)</scene>.  The <scene name='51/516475/Cv/6'>active site is located between the synthetase domain and D2 domain and covered by the LID motif</scene>.  <scene name='51/516475/Cv/9'>Whole active site</scene>. N-terminal glutaminase domain contains <scene name='51/516475/Cv/11'>TextToBeDisplayed</scene><ref>PMID:23816837</ref>.
Human GMPS structure contains <scene name='51/516475/Cv/10'>2 dimerization domains (D1 and D2)</scene>.  The <scene name='51/516475/Cv/6'>active site is located between the synthetase domain and D2 domain and covered by the LID motif</scene>.  <scene name='51/516475/Cv/9'>Whole active site</scene>. N-terminal glutaminase domain contains <scene name='51/516475/Cv/11'>catalytic triad Cys104, His190, Glu192</scene><ref>PMID:23816837</ref>.


==3D structures of GMP synthase==
==3D structures of GMP synthase==

Revision as of 12:40, 21 March 2016

Function

GMP synthase (GMPS) catalyzes the conversion of xantosine 5’-phosphate (XMP), ATP, glutamine and water to glutamate, GMP, AMP and diphosphate. GMPS is active in purine and glutamate metabolism[1]. GMPS is a bifunctional two-domain enzyme with the dominates extracts ammonia from glutamine and the adds amine group to XMP to produce GMP.

Structural highlights

Human GMPS structure contains . The . . N-terminal glutaminase domain contains [2].

3D structures of GMP synthase

Updated on 05-May-2025

1wl8, 2d7j – PhGMPS subunit A – Pyrococcus horikoshii

2dpl, 3a4i - PhGMPS subunit B
2ywb – TtGMPS – Thermus thermophilus
3tqi – GMPS – Coxiella burnetii
1kxj – TmGMPS – Thermotoga maritima
2a9v – GMPS – Thermoplasma acidophilum
2lxn – GMPS subunit A – Methanocaldococcus jannaschii
2vpi – hGMPS glutaminase domain – human
2vxo - hGMPS + XMP
2ywc – TtGMPS + XMP
2iss – TmGMPS subunit PDXT + PLP biosynthesis lyase PDXS
1gpm – GMPS + pyrophosphate + AMP – Escherichia coli

References

  1. ↑ Reddy BA, van der Knaap JA, Bot AG, Mohd-Sarip A, Dekkers DH, Timmermans MA, Martens JW, Demmers JA, Verrijzer CP. Nucleotide biosynthetic enzyme GMP synthase is a TRIM21-controlled relay of p53 stabilization. Mol Cell. 2014 Feb 6;53(3):458-70. doi: 10.1016/j.molcel.2013.12.017. Epub 2014, Jan 23. PMID:24462112 doi:http://dx.doi.org/10.1016/j.molcel.2013.12.017
  2. ↑ Welin M, Lehtio L, Johansson A, Flodin S, Nyman T, Tresaugues L, Hammarstrom M, Graslund S, Nordlund P. Substrate Specificity and Oligomerization of Human GMP Synthetase. J Mol Biol. 2013 Jun 28. pii: S0022-2836(13)00427-0. doi:, 10.1016/j.jmb.2013.06.032. PMID:23816837 doi:10.1016/j.jmb.2013.06.032

Structure of human GMP synthase dimer complex with xantosine 5-phosphate and sulfate (PDB entry 2vxo)

Drag the structure with the mouse to rotate

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Michal Harel, Alexander Berchansky
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