4rc1

From Proteopedia

(Difference between revisions)

Current revision

Structure of the methanofuran/methanopterin biosynthetic enzyme MJ1099 from Methanocaldococcus jannaschii with PRPP

Structural highlights

4rc1 is a 9 chain structure with sequence from Methanocaldococcus jannaschii DSM 2661. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.4Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MFNB_METJA Catalyzes the formation of 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate (4-HFC-P) from two molecules of glyceraldehyde-3-P (GA-3-P).[HAMAP-Rule:MF_00681]^[1] ^[2]

Publication Abstract from PubMed

Prior studies have indicated that MJ1099 from Methanocaldococcus jannaschii has roles in the biosynthesis of tetrahydromethanopterin and methanofuran, two key cofactors of one-carbon (C1) metabolism in diverse organisms including the methanogenic archaea. Here, the structure of MJ1099 has been solved to 1.7 A resolution using anomalous scattering methods. The results indicate that MJ1099 is a member of the TIM-barrel superfamily and that it is a homohexamer. Bioinformatic analyses identified a potential active site that is highly conserved among MJ1099 homologs and the key amino acids involved were identified. The results presented here should guide further studies of MJ1099 including mechanistic studies and possibly the development of inhibitors that target the methanogenic archaea in the digestive tracts of humans and that are a source of the greenhouse gas methane.

Structure of the methanofuran/methanopterin-biosynthetic enzyme MJ1099 from Methanocaldococcus jannaschii.,Bobik TA, Morales EJ, Shin A, Cascio D, Sawaya MR, Arbing M, Yeates TO, Rasche ME Acta Crystallogr F Struct Biol Commun. 2014 Nov;70(Pt 11):1472-9. doi:, 10.1107/S2053230X1402130X. Epub 2014 Oct 25. PMID:25372812^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Miller D, Wang Y, Xu H, Harich K, White RH. Biosynthesis of the 5-(Aminomethyl)-3-furanmethanol moiety of methanofuran. Biochemistry. 2014 Jul 22;53(28):4635-47. PMID:24977328 doi:10.1021/bi500615p
↑ Wang Y, Jones MK, Xu H, Ray WK, White RH. Mechanism of the Enzymatic Synthesis of 4-(Hydroxymethyl)-2- furancarboxaldehyde-phosphate (4-HFC-P) from Glyceraldehyde-3-phosphate Catalyzed by 4-HFC-P Synthase. Biochemistry. 2015 May 19;54(19):2997-3008. PMID:25905665 doi:10.1021/acs.biochem.5b00176
↑ Bobik TA, Morales EJ, Shin A, Cascio D, Sawaya MR, Arbing M, Yeates TO, Rasche ME. Structure of the methanofuran/methanopterin-biosynthetic enzyme MJ1099 from Methanocaldococcus jannaschii. Acta Crystallogr F Struct Biol Commun. 2014 Nov;70(Pt 11):1472-9. doi:, 10.1107/S2053230X1402130X. Epub 2014 Oct 25. PMID:25372812 doi:http://dx.doi.org/10.1107/S2053230X1402130X

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4rc1"

@@ Line 1: / Line 1: @@
 ==Structure of the methanofuran/methanopterin biosynthetic enzyme MJ1099 from Methanocaldococcus jannaschii with PRPP==
-<StructureSection load='4rc1' size='340' side='right' caption='[[4rc1]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+<StructureSection load='4rc1' size='340' side='right'caption='[[4rc1]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4rc1]] is a 9 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RC1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RC1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4rc1]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii_DSM_2661 Methanocaldococcus jannaschii DSM 2661]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RC1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RC1 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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]] 2.4&#8491;</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=4rc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rc1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rc1 RCSB], [http://www.ebi.ac.uk/pdbsum/4rc1 PDBsum]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=4rc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rc1 OCA], [https://pdbe.org/4rc1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rc1 RCSB], [https://www.ebi.ac.uk/pdbsum/4rc1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rc1 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/MFNB_METJA MFNB_METJA] Catalyzes the formation of 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate (4-HFC-P) from two molecules of glyceraldehyde-3-P (GA-3-P).[HAMAP-Rule:MF_00681]<ref>PMID:24977328</ref> <ref>PMID:25905665</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 14: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4rc1" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Bobik, T A]]
+[[Category: Large Structures]]
-[[Category: Cascio, D]]
+[[Category: Methanocaldococcus jannaschii DSM 2661]]
-[[Category: Morales, E J]]
+[[Category: Bobik TA]]
-[[Category: Rasche, M E]]
+[[Category: Cascio D]]
-[[Category: Sawaya, M R]]
+[[Category: Morales EJ]]
-[[Category: Yeates, T O]]
+[[Category: Rasche ME]]
-[[Category: Dihydromethanopterin reductase]]
+[[Category: Sawaya MR]]
-[[Category: Flavin]]
+[[Category: Yeates TO]]
-[[Category: Methanopterin]]
-[[Category: Protein cage]]
-[[Category: Unknown function]]

4rc1

From Proteopedia

Current revision

Structure of the methanofuran/methanopterin biosynthetic enzyme MJ1099 from Methanocaldococcus jannaschii with PRPP

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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