8dyl: Difference between revisions

Latest revision as of 15:05, 13 August 2026

Crystal structure of human methylmalonyl-CoA mutase bound to aquocobalamin

Structural highlights

8dyl is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.9Å
Ligands:	GOL
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

MUTA_HUMAN Defects in MUT are the cause of methylmalonic aciduria type mut (MMAM) [MIM:251000. MMAM is an often fatal disorder of organic acid metabolism. Common clinical features include lethargy, vomiting, failure to thrive, hypotonia, neurological deficit and early death. Two forms of the disease are distinguished by the presence (mut-) or absence (mut0) of residual enzyme activity. Mut0 patients have more severe neurological manifestations of the disease than do MUT- patients. MMAM is unresponsive to vitamin B12 therapy.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8] ^[9] ^[10] ^[11] ^[12] ^[13] ^[14]

Function

MUTA_HUMAN Involved in the degradation of several amino acids, odd-chain fatty acids and cholesterol via propionyl-CoA to the tricarboxylic acid cycle. MCM has different functions in other species.

References

↑ Jansen R, Ledley FD. Heterozygous mutations at the mut locus in fibroblasts with mut0 methylmalonic acidemia identified by polymerase-chain-reaction cDNA cloning. Am J Hum Genet. 1990 Nov;47(5):808-14. PMID:1977311
↑ Raff ML, Crane AM, Jansen R, Ledley FD, Rosenblatt DS. Genetic characterization of a MUT locus mutation discriminating heterogeneity in mut0 and mut- methylmalonic aciduria by interallelic complementation. J Clin Invest. 1991 Jan;87(1):203-7. PMID:1670635 doi:https://dx.doi.org/10.1172/JCI114972
↑ Crane AM, Martin LS, Valle D, Ledley FD. Phenotype of disease in three patients with identical mutations in methylmalonyl CoA mutase. Hum Genet. 1992 May;89(3):259-64. PMID:1351030
↑ Crane AM, Jansen R, Andrews ER, Ledley FD. Cloning and expression of a mutant methylmalonyl coenzyme A mutase with altered cobalamin affinity that causes mut- methylmalonic aciduria. J Clin Invest. 1992 Feb;89(2):385-91. PMID:1346616 doi:https://dx.doi.org/10.1172/JCI115597
↑ Crane AM, Ledley FD. Clustering of mutations in methylmalonyl CoA mutase associated with mut- methylmalonic acidemia. Am J Hum Genet. 1994 Jul;55(1):42-50. PMID:7912889
↑ Qureshi AA, Crane AM, Matiaszuk NV, Rezvani I, Ledley FD, Rosenblatt DS. Cloning and expression of mutations demonstrating intragenic complementation in mut0 methylmalonic aciduria. J Clin Invest. 1994 Apr;93(4):1812-9. PMID:7909321 doi:https://dx.doi.org/10.1172/JCI117166
↑ Janata J, Kogekar N, Fenton WA. Expression and kinetic characterization of methylmalonyl-CoA mutase from patients with the mut- phenotype: evidence for naturally occurring interallelic complementation. Hum Mol Genet. 1997 Sep;6(9):1457-64. PMID:9285782
↑ Adjalla CE, Hosack AR, Matiaszuk NV, Rosenblatt DS. A common mutation among blacks with mut- methylmalonic aciduria. Hum Mutat. 1998;Suppl 1:S248-50. PMID:9452100
↑ Adjalla CE, Hosack AR, Gilfix BM, Lamothe E, Sun S, Chan A, Evans S, Matiaszuk NV, Rosenblatt DS. Seven novel mutations in mut methylmalonic aciduria. Hum Mutat. 1998;11(4):270-4. PMID:9554742 doi:<270::AID-HUMU3>3.0.CO;2-T 10.1002/(SICI)1098-1004(1998)11:4<270::AID-HUMU3>3.0.CO;2-T
↑ Fuchshuber A, Mucha B, Baumgartner ER, Vollmer M, Hildebrandt F. mut0 methylmalonic acidemia: eleven novel mutations of the methylmalonyl CoA mutase including a deletion-insertion mutation. Hum Mutat. 2000 Aug;16(2):179. PMID:10923046 doi:<179::AID-HUMU17>3.0.CO;2-R 10.1002/1098-1004(200008)16:2<179::AID-HUMU17>3.0.CO;2-R
↑ Berger I, Shaag A, Anikster Y, Baumgartner ER, Bar-Meir M, Joseph A, Elpeleg ON. Mutation analysis of the MCM gene in Israeli patients with mut(0) disease. Mol Genet Metab. 2001 May;73(1):107-10. PMID:11350191 doi:10.1006/mgme.2001.3166
↑ Acquaviva C, Benoist JF, Pereira S, Callebaut I, Koskas T, Porquet D, Elion J. Molecular basis of methylmalonyl-CoA mutase apoenzyme defect in 40 European patients affected by mut(o) and mut- forms of methylmalonic acidemia: identification of 29 novel mutations in the MUT gene. Hum Mutat. 2005 Feb;25(2):167-76. PMID:15643616 doi:10.1002/humu.20128
↑ Martinez MA, Rincon A, Desviat LR, Merinero B, Ugarte M, Perez B. Genetic analysis of three genes causing isolated methylmalonic acidemia: identification of 21 novel allelic variants. Mol Genet Metab. 2005 Apr;84(4):317-25. Epub 2005 Jan 22. PMID:15781192 doi:S1096-7192(04)00307-5
↑ Worgan LC, Niles K, Tirone JC, Hofmann A, Verner A, Sammak A, Kucic T, Lepage P, Rosenblatt DS. Spectrum of mutations in mut methylmalonic acidemia and identification of a common Hispanic mutation and haplotype. Hum Mutat. 2006 Jan;27(1):31-43. PMID:16281286 doi:10.1002/humu.20258

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OCA

[1] Jansen R, Ledley FD. Heterozygous mutations at the mut locus in fibroblasts with mut0 methylmalonic acidemia identified by polymerase-chain-reaction cDNA cloning. Am J Hum Genet. 1990 Nov;47(5):808-14. PMID:1977311

[2] Raff ML, Crane AM, Jansen R, Ledley FD, Rosenblatt DS. Genetic characterization of a MUT locus mutation discriminating heterogeneity in mut0 and mut- methylmalonic aciduria by interallelic complementation. J Clin Invest. 1991 Jan;87(1):203-7. PMID:1670635 doi:https://dx.doi.org/10.1172/JCI114972

[3] Crane AM, Martin LS, Valle D, Ledley FD. Phenotype of disease in three patients with identical mutations in methylmalonyl CoA mutase. Hum Genet. 1992 May;89(3):259-64. PMID:1351030

[4] Crane AM, Jansen R, Andrews ER, Ledley FD. Cloning and expression of a mutant methylmalonyl coenzyme A mutase with altered cobalamin affinity that causes mut- methylmalonic aciduria. J Clin Invest. 1992 Feb;89(2):385-91. PMID:1346616 doi:https://dx.doi.org/10.1172/JCI115597

[5] Crane AM, Ledley FD. Clustering of mutations in methylmalonyl CoA mutase associated with mut- methylmalonic acidemia. Am J Hum Genet. 1994 Jul;55(1):42-50. PMID:7912889

[6] Qureshi AA, Crane AM, Matiaszuk NV, Rezvani I, Ledley FD, Rosenblatt DS. Cloning and expression of mutations demonstrating intragenic complementation in mut0 methylmalonic aciduria. J Clin Invest. 1994 Apr;93(4):1812-9. PMID:7909321 doi:https://dx.doi.org/10.1172/JCI117166

[7] Janata J, Kogekar N, Fenton WA. Expression and kinetic characterization of methylmalonyl-CoA mutase from patients with the mut- phenotype: evidence for naturally occurring interallelic complementation. Hum Mol Genet. 1997 Sep;6(9):1457-64. PMID:9285782

[8] Adjalla CE, Hosack AR, Matiaszuk NV, Rosenblatt DS. A common mutation among blacks with mut- methylmalonic aciduria. Hum Mutat. 1998;Suppl 1:S248-50. PMID:9452100

[9] Adjalla CE, Hosack AR, Gilfix BM, Lamothe E, Sun S, Chan A, Evans S, Matiaszuk NV, Rosenblatt DS. Seven novel mutations in mut methylmalonic aciduria. Hum Mutat. 1998;11(4):270-4. PMID:9554742 doi:<270::AID-HUMU3>3.0.CO;2-T 10.1002/(SICI)1098-1004(1998)11:4<270::AID-HUMU3>3.0.CO;2-T

[10] Fuchshuber A, Mucha B, Baumgartner ER, Vollmer M, Hildebrandt F. mut0 methylmalonic acidemia: eleven novel mutations of the methylmalonyl CoA mutase including a deletion-insertion mutation. Hum Mutat. 2000 Aug;16(2):179. PMID:10923046 doi:<179::AID-HUMU17>3.0.CO;2-R 10.1002/1098-1004(200008)16:2<179::AID-HUMU17>3.0.CO;2-R

[11] Berger I, Shaag A, Anikster Y, Baumgartner ER, Bar-Meir M, Joseph A, Elpeleg ON. Mutation analysis of the MCM gene in Israeli patients with mut(0) disease. Mol Genet Metab. 2001 May;73(1):107-10. PMID:11350191 doi:10.1006/mgme.2001.3166

[12] Acquaviva C, Benoist JF, Pereira S, Callebaut I, Koskas T, Porquet D, Elion J. Molecular basis of methylmalonyl-CoA mutase apoenzyme defect in 40 European patients affected by mut(o) and mut- forms of methylmalonic acidemia: identification of 29 novel mutations in the MUT gene. Hum Mutat. 2005 Feb;25(2):167-76. PMID:15643616 doi:10.1002/humu.20128

[13] Martinez MA, Rincon A, Desviat LR, Merinero B, Ugarte M, Perez B. Genetic analysis of three genes causing isolated methylmalonic acidemia: identification of 21 novel allelic variants. Mol Genet Metab. 2005 Apr;84(4):317-25. Epub 2005 Jan 22. PMID:15781192 doi:S1096-7192(04)00307-5

[14] Worgan LC, Niles K, Tirone JC, Hofmann A, Verner A, Sammak A, Kucic T, Lepage P, Rosenblatt DS. Spectrum of mutations in mut methylmalonic acidemia and identification of a common Hispanic mutation and haplotype. Hum Mutat. 2006 Jan;27(1):31-43. PMID:16281286 doi:10.1002/humu.20258

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 8dyl is ON HOLD
+==Crystal structure of human methylmalonyl-CoA mutase bound to aquocobalamin==
+<StructureSection load='8dyl' size='340' side='right'caption='[[8dyl]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
-Authors: Mascarenhas, R.N., Gouda, H., Banerjee, R.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8dyl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8DYL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DYL FirstGlance]. <br>
-Description: Crystal structure of human methylmalonyl-CoA mutase bound to aquocobalamin
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
-[[Category: Unreleased Structures]]
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-[[Category: Gouda, H]]
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8dyl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dyl OCA], [https://pdbe.org/8dyl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dyl RCSB], [https://www.ebi.ac.uk/pdbsum/8dyl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dyl ProSAT]</span></td></tr>
-[[Category: Mascarenhas, R.N]]
+</table>
-[[Category: Banerjee, R]]
+== Disease ==
+[https://www.uniprot.org/uniprot/MUTA_HUMAN MUTA_HUMAN] Defects in MUT are the cause of methylmalonic aciduria type mut (MMAM) [MIM:[https://omim.org/entry/251000 251000]. MMAM is an often fatal disorder of organic acid metabolism. Common clinical features include lethargy, vomiting, failure to thrive, hypotonia, neurological deficit and early death. Two forms of the disease are distinguished by the presence (mut-) or absence (mut0) of residual enzyme activity. Mut0 patients have more severe neurological manifestations of the disease than do MUT- patients. MMAM is unresponsive to vitamin B12 therapy.<ref>PMID:1977311</ref> <ref>PMID:1670635</ref> <ref>PMID:1351030</ref> <ref>PMID:1346616</ref> <ref>PMID:7912889</ref> <ref>PMID:7909321</ref> <ref>PMID:9285782</ref> <ref>PMID:9452100</ref> <ref>PMID:9554742</ref> <ref>PMID:10923046</ref> <ref>PMID:11350191</ref> <ref>PMID:15643616</ref> <ref>PMID:15781192</ref> <ref>PMID:16281286</ref>
+== Function ==
+[https://www.uniprot.org/uniprot/MUTA_HUMAN MUTA_HUMAN] Involved in the degradation of several amino acids, odd-chain fatty acids and cholesterol via propionyl-CoA to the tricarboxylic acid cycle. MCM has different functions in other species.
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Banerjee R]]
+[[Category: Gouda H]]
+[[Category: Mascarenhas RN]]

8dyl: Difference between revisions

Latest revision as of 15:05, 13 August 2026

Crystal structure of human methylmalonyl-CoA mutase bound to aquocobalamin

Structural highlights

Disease

Function

References

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