1mj4: Difference between revisions

Latest revision as of 06:37, 13 August 2026

Crystal Structure Analysis of the cytochrome b5 domain of human sulfite oxidase

Structural highlights

1mj4 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 1.2Å
Ligands:	GOL, HEM, SO4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

SUOX_HUMAN Defects in SUOX are the cause of isolated sulfite oxidase deficiency (ISOD) [MIM:272300; also known as sulfocysteinuria. ISOD is characterized by neurological abnormalities including multicystic leukoencephalopathy with brain atrophy. Patients often suffer from seizures. Often leads to death at an early age.^[1] ^[2] ^[3] ^[4] ^[5]

Function

SUOX_HUMAN

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The molybdenum- and iron-containing enzyme sulfite oxidase catalyzes the physiologically vital oxidation of sulfite to sulfate. Sulfite oxidase contains three domains: an N-terminal cytochrome b(5) domain, a central domain harboring the molybdenum cofactor (Moco) and a C-terminal dimerization domain. Oxidation of the substrate sulfite is coupled to the transfer of two electrons to the molybdenum cofactor. Subsequently, these electrons are passed on, one at a time, to the b(5) heme of sulfite oxidase and from there to the soluble electron carrier cytochrome c. The crystal structure of the oxidized human sulfite oxidase cytochrome b(5) domain has been determined at 1.2 A resolution and has been refined to a crystallographic R factor of 0.107 (R(free) = 0.137). A comparison of this structure with other b(5)-type cytochromes reveals distinct structural features present in the sulfite oxidase b(5) domain which promote optimal electron transport between the Moco of sulfite oxidase and the heme of cytochrome c.

The 1.2 A structure of the human sulfite oxidase cytochrome b(5) domain.,Rudolph MJ, Johnson JL, Rajagopalan KV, Kisker C Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1183-91. Epub 2003, Jun 27. PMID:12832761^[6]

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

References

↑ Kisker C, Schindelin H, Pacheco A, Wehbi WA, Garrett RM, Rajagopalan KV, Enemark JH, Rees DC. Molecular basis of sulfite oxidase deficiency from the structure of sulfite oxidase. Cell. 1997 Dec 26;91(7):973-83. PMID:9428520
↑ Garrett RM, Johnson JL, Graf TN, Feigenbaum A, Rajagopalan KV. Human sulfite oxidase R160Q: identification of the mutation in a sulfite oxidase-deficient patient and expression and characterization of the mutant enzyme. Proc Natl Acad Sci U S A. 1998 May 26;95(11):6394-8. PMID:9600976
↑ Edwards MC, Johnson JL, Marriage B, Graf TN, Coyne KE, Rajagopalan KV, MacDonald IM. Isolated sulfite oxidase deficiency: review of two cases in one family. Ophthalmology. 1999 Oct;106(10):1957-61. PMID:10519592 doi:S0161-6420(99)90408-6
↑ Johnson JL, Coyne KE, Garrett RM, Zabot MT, Dorche C, Kisker C, Rajagopalan KV. Isolated sulfite oxidase deficiency: identification of 12 novel SUOX mutations in 10 patients. Hum Mutat. 2002 Jul;20(1):74. PMID:12112661 doi:10.1002/humu.9038
↑ Lee HF, Mak BS, Chi CS, Tsai CR, Chen CH, Shu SG. A novel mutation in neonatal isolated sulphite oxidase deficiency. Neuropediatrics. 2002 Aug;33(4):174-9. PMID:12368985 doi:10.1055/s-2002-34491
↑ Rudolph MJ, Johnson JL, Rajagopalan KV, Kisker C. The 1.2 A structure of the human sulfite oxidase cytochrome b(5) domain. Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1183-91. Epub 2003, Jun 27. PMID:12832761

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Kisker C, Schindelin H, Pacheco A, Wehbi WA, Garrett RM, Rajagopalan KV, Enemark JH, Rees DC. Molecular basis of sulfite oxidase deficiency from the structure of sulfite oxidase. Cell. 1997 Dec 26;91(7):973-83. PMID:9428520

[2] Garrett RM, Johnson JL, Graf TN, Feigenbaum A, Rajagopalan KV. Human sulfite oxidase R160Q: identification of the mutation in a sulfite oxidase-deficient patient and expression and characterization of the mutant enzyme. Proc Natl Acad Sci U S A. 1998 May 26;95(11):6394-8. PMID:9600976

[3] Edwards MC, Johnson JL, Marriage B, Graf TN, Coyne KE, Rajagopalan KV, MacDonald IM. Isolated sulfite oxidase deficiency: review of two cases in one family. Ophthalmology. 1999 Oct;106(10):1957-61. PMID:10519592 doi:S0161-6420(99)90408-6

[4] Johnson JL, Coyne KE, Garrett RM, Zabot MT, Dorche C, Kisker C, Rajagopalan KV. Isolated sulfite oxidase deficiency: identification of 12 novel SUOX mutations in 10 patients. Hum Mutat. 2002 Jul;20(1):74. PMID:12112661 doi:10.1002/humu.9038

[5] Lee HF, Mak BS, Chi CS, Tsai CR, Chen CH, Shu SG. A novel mutation in neonatal isolated sulphite oxidase deficiency. Neuropediatrics. 2002 Aug;33(4):174-9. PMID:12368985 doi:10.1055/s-2002-34491

[6] Rudolph MJ, Johnson JL, Rajagopalan KV, Kisker C. The 1.2 A structure of the human sulfite oxidase cytochrome b(5) domain. Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1183-91. Epub 2003, Jun 27. PMID:12832761

[1]

[2]

[3]

[4]

[5]

[6]

@@ Line 3: / Line 3: @@
 <StructureSection load='1mj4' size='340' side='right'caption='[[1mj4]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1mj4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MJ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MJ4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1mj4]] 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=1MJ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MJ4 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.2&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1sox|1sox]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Sulfite_oxidase Sulfite oxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.3.1 1.8.3.1] </span></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=1mj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mj4 OCA], [https://pdbe.org/1mj4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mj4 RCSB], [https://www.ebi.ac.uk/pdbsum/1mj4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mj4 ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[https://www.uniprot.org/uniprot/SUOX_HUMAN SUOX_HUMAN]] Defects in SUOX are the cause of isolated sulfite oxidase deficiency (ISOD) [MIM:[https://omim.org/entry/272300 272300]]; also known as sulfocysteinuria. ISOD is characterized by neurological abnormalities including multicystic leukoencephalopathy with brain atrophy. Patients often suffer from seizures. Often leads to death at an early age.<ref>PMID:9428520</ref> <ref>PMID:9600976</ref> <ref>PMID:10519592</ref> <ref>PMID:12112661</ref> <ref>PMID:12368985</ref>
+[https://www.uniprot.org/uniprot/SUOX_HUMAN SUOX_HUMAN] Defects in SUOX are the cause of isolated sulfite oxidase deficiency (ISOD) [MIM:[https://omim.org/entry/272300 272300]; also known as sulfocysteinuria. ISOD is characterized by neurological abnormalities including multicystic leukoencephalopathy with brain atrophy. Patients often suffer from seizures. Often leads to death at an early age.<ref>PMID:9428520</ref> <ref>PMID:9600976</ref> <ref>PMID:10519592</ref> <ref>PMID:12112661</ref> <ref>PMID:12368985</ref>
+== Function ==
+[https://www.uniprot.org/uniprot/SUOX_HUMAN SUOX_HUMAN]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 16: / Line 17: @@
    <jmolCheckbox>
      <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mj/1mj4_consurf.spt"</scriptWhenChecked>
-     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
    </jmolCheckbox>
@@ Line 37: / Line 38: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Sulfite oxidase]]
+[[Category: Johnson JL]]
-[[Category: Johnson, J L]]
+[[Category: Kisker C]]
-[[Category: Kisker, C]]
+[[Category: Rajagopalan KV]]
-[[Category: Rajagopalan, K V]]
+[[Category: Rudolph MJ]]
-[[Category: Rudolph, M J]]
-[[Category: Cytochrome b5]]
-[[Category: Heme]]
-[[Category: Oxidoreductase]]

1mj4: Difference between revisions

Latest revision as of 06:37, 13 August 2026

Crystal Structure Analysis of the cytochrome b5 domain of human sulfite oxidase

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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