4coo

From Proteopedia

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Current revision

Crystal structure of human cystathionine beta-synthase (delta516-525) at 2.0 angstrom resolution

Structural highlights

4coo is a 2 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 2Å
Ligands:	, , , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

CBS_HUMAN Defects in CBS are the cause of cystathionine beta-synthase deficiency (CBSD) [MIM:236200. CBSD is an enzymatic deficiency resulting in altered sulfur metabolism and homocystinuria. The clinical features of untreated homocystinuria due to CBS deficiency include myopia, ectopia lentis, mental retardation, skeletal anomalies resembling Marfan syndrome, and thromboembolic events. Light skin and hair can also be present. Biochemical features include increased urinary homocystine and methionine.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8] ^[9] ^[10] ^[11] ^[12] ^[13] ^[14] ^[15] ^[16] ^[17] ^[18] ^[19] ^[20] ^[21] ^[22] ^[23] ^[24] ^[25] ^[26] ^[27] ^[28] ^[29] ^[30] ^[31] ^[32] ^[33] ^[34] ^[35]

Function

CBS_HUMAN Only known pyridoxal phosphate-dependent enzyme that contains heme. Important regulator of hydrogen sulfide, especially in the brain, utilizing cysteine instead of serine to catalyze the formation of hydrogen sulfide. Hydrogen sulfide is a gastratransmitter with signaling and cytoprotective effects such as acting as a neuromodulator in the brain to protect neurons against hypoxic injury (By similarity).

Publication Abstract from PubMed

Cystathionine beta-synthase (CBS) is a key enzyme in sulphur metabolism, and its inherited deficiency causes homocystinuria. Mammalian CBS is modulated by the binding of S-adenosyl-L-methionine (SAM) to its regulatory domain, which activates its catalytic domain. To investigate the underlying mechanism, we performed x-ray crystallography, mutagenesis and mass-spectrometry (MS) on human CBS. The 1.7 A structure of a SAM-bound CBS regulatory domain shows one SAM molecule per monomer, at the interface between two constituent modules (CBS-1, CBS-2). SAM binding is accompanied by a reorientation between the two modules, relative to the SAM-free basal state, to form interactions with SAM via residues verified by mutagenesis to be important for SAM binding (Phe443, Asp444, Gln445 and Asp538) and for SAM-driven inter-domain communication (Phe443, Asp538). The observed structural change is further supported by ion mobility MS showing that as-purified CBS exists in two conformational populations which converged to one upon binding SAM. We therefore propose that SAM-induced conformational change alters the interface and arrangement between the catalytic and regulatory domains within the CBS oligomer, thereby increasing the accessibility of the enzyme active site for catalysis.

Inter-Domain Communication Of Human Cystathionine Beta Synthase: Structural Basis Of S-Adenosyl-L-Methionine Activation.,McCorvie TJ, Kopec J, Hyung SJ, Fitzpatrick F, Feng X, Termine D, Strain-Damerell C, Vollmar M, Fleming J, Janz JM, Bulawa C, Yue WW J Biol Chem. 2014 Oct 21. pii: jbc.M114.610782. PMID:25336647^[36]

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

References

↑ Kozich V, Kraus JP. Screening for mutations by expressing patient cDNA segments in E. coli: homocystinuria due to cystathionine beta-synthase deficiency. Hum Mutat. 1992;1(2):113-23. PMID:1301198 doi:http://dx.doi.org/10.1002/humu.1380010206
↑ Kozich V, de Franchis R, Kraus JP. Molecular defect in a patient with pyridoxine-responsive homocystinuria. Hum Mol Genet. 1993 Jun;2(6):815-6. PMID:8353501
↑ Hu FL, Gu Z, Kozich V, Kraus JP, Ramesh V, Shih VE. Molecular basis of cystathionine beta-synthase deficiency in pyridoxine responsive and nonresponsive homocystinuria. Hum Mol Genet. 1993 Nov;2(11):1857-60. PMID:7506602
↑ de Franchis R, Kozich V, McInnes RR, Kraus JP. Identical genotypes in siblings with different homocystinuric phenotypes: identification of three mutations in cystathionine beta-synthase using an improved bacterial expression system. Hum Mol Genet. 1994 Jul;3(7):1103-8. PMID:7981678
↑ Marble M, Geraghty MT, de Franchis R, Kraus JP, Valle D. Characterization of a cystathionine beta-synthase allele with three mutations in cis in a patient with B6 nonresponsive homocystinuria. Hum Mol Genet. 1994 Oct;3(10):1883-6. PMID:7849717
↑ Kraus JP. Komrower Lecture. Molecular basis of phenotype expression in homocystinuria. J Inherit Metab Dis. 1994;17(4):383-90. PMID:7967489
↑ Shih VE, Fringer JM, Mandell R, Kraus JP, Berry GT, Heidenreich RA, Korson MS, Levy HL, Ramesh V. A missense mutation (I278T) in the cystathionine beta-synthase gene prevalent in pyridoxine-responsive homocystinuria and associated with mild clinical phenotype. Am J Hum Genet. 1995 Jul;57(1):34-9. PMID:7611293
↑ Sebastio G, Sperandeo MP, Panico M, de Franchis R, Kraus JP, Andria G. The molecular basis of homocystinuria due to cystathionine beta-synthase deficiency in Italian families, and report of four novel mutations. Am J Hum Genet. 1995 Jun;56(6):1324-33. PMID:7762555
↑ Kluijtmans LA, Blom HJ, Boers GH, van Oost BA, Trijbels FJ, van den Heuvel LP. Two novel missense mutations in the cystathionine beta-synthase gene in homocystinuric patients. Hum Genet. 1995 Aug;96(2):249-50. PMID:7635485
↑ Kruger WD, Cox DR. A yeast assay for functional detection of mutations in the human cystathionine beta-synthase gene. Hum Mol Genet. 1995 Jul;4(7):1155-61. PMID:8528202
↑ Sperandeo MP, Panico M, Pepe A, Candito M, de Franchis R, Kraus JP, Andria G, Sebastio G. Molecular analysis of patients affected by homocystinuria due to cystathionine beta-synthase deficiency: report of a new mutation in exon 8 and a deletion in intron 11. J Inherit Metab Dis. 1995;18(2):211-4. PMID:7564249
↑ Kluijtmans LA, Boers GH, Stevens EM, Renier WO, Kraus JP, Trijbels FJ, van den Heuvel LP, Blom HJ. Defective cystathionine beta-synthase regulation by S-adenosylmethionine in a partially pyridoxine responsive homocystinuria patient. J Clin Invest. 1996 Jul 15;98(2):285-9. PMID:8755636 doi:10.1172/JCI118791
↑ Sperandeo MP, Candito M, Sebastio G, Rolland MO, Turc-Carel C, Giudicelli H, Dellamonica P, Andria G. Homocysteine response to methionine challenge in four obligate heterozygotes for homocystinuria and relationship with cystathionine beta-synthase mutations. J Inherit Metab Dis. 1996;19(3):351-6. PMID:8803779
↑ Dawson PA, Cox AJ, Emmerson BT, Dudman NP, Kraus JP, Gordon RB. Characterisation of five missense mutations in the cystathionine beta-synthase gene from three patients with B6-nonresponsive homocystinuria. Eur J Hum Genet. 1997 Jan-Feb;5(1):15-21. PMID:9156316
↑ Kim CE, Gallagher PM, Guttormsen AB, Refsum H, Ueland PM, Ose L, Folling I, Whitehead AS, Tsai MY, Kruger WD. Functional modeling of vitamin responsiveness in yeast: a common pyridoxine-responsive cystathionine beta-synthase mutation in homocystinuria. Hum Mol Genet. 1997 Dec;6(13):2213-21. PMID:9361025
↑ Aral B, Coude M, London J, Aupetit J, Chasse JF, Zabot MT, Chadefaux-Vekemans B, Kamoun P. Two novel mutations (K384E and L539S) in the C-terminal moiety of the cystathionine beta-synthase protein in two French pyridoxine-responsive homocystinuria patients. Hum Mutat. 1997;9(1):81-2. PMID:8990018 doi:<81::AID-HUMU18>3.0.CO;2-L 10.1002/(SICI)1098-1004(1997)9:1<81::AID-HUMU18>3.0.CO;2-L
↑ Kozich V, Janosik M, Sokolova J, Oliveriusova J, Orendac M, Kraus JP, Elleder D. Analysis of CBS alleles in Czech and Slovak patients with homocystinuria: report on three novel mutations E176K, W409X and 1223 + 37 del99. J Inherit Metab Dis. 1997 Jul;20(3):363-6. PMID:9266356
↑ Tsai MY, Wong PW, Garg U, Hanson NQ, Schwichtenberg K. Two Novel Mutations in the Cystathionine beta-synthase Gene of Homocystinuric Patients. Mol Diagn. 1997 Jun;2(2):129-133. PMID:10462600 doi:10.1054/MODI00200129
↑ Gordon RB, Cox AJ, Dawson PA, Emmerson BT, Kraus JP, Dudman NP. Mutational analysis of the cystathionine beta-synthase gene: a splicing mutation, two missense mutations and an insertion in patients with homocystinuria. Mutations in brief no. 120. Online. Hum Mutat. 1998;11(4):332. PMID:10215408 doi:<332::AID-HUMU16>3.0.CO;2-P 10.1002/(SICI)1098-1004(1998)11:4<332::AID-HUMU16>3.0.CO;2-P
↑ Gallagher PM, Naughten E, Hanson NQ, Schwichtenberg K, Bignell M, Yuan M, Ward P, Yap S, Whitehead AS, Tsai MY. Characterization of mutations in the cystathionine beta-synthase gene in Irish patients with homocystinuria. Mol Genet Metab. 1998 Dec;65(4):298-302. PMID:9889017 doi:10.1006/mgme.1998.2771
↑ de Franchis R, Kraus E, Kozich V, Sebastio G, Kraus JP. Four novel mutations in the cystathionine beta-synthase gene: effect of a second linked mutation on the severity of the homocystinuric phenotype. Hum Mutat. 1999;13(6):453-7. PMID:10408774 doi:<453::AID-HUMU4>3.0.CO;2-K 10.1002/(SICI)1098-1004(1999)13:6<453::AID-HUMU4>3.0.CO;2-K
↑ Gat-Yablonski G, Mandel H, Fowler B, Taleb O, Sela BA. Homocystinuria in the Arab population of Israel: identification of two novel mutations using DGGE analysis. Hum Mutat. 2000 Oct;16(4):372. PMID:11013450 doi:<372::AID-HUMU12>3.0.CO;2-J 10.1002/1098-1004(200010)16:4<372::AID-HUMU12>3.0.CO;2-J
↑ Janosik M, Oliveriusova J, Janosikova B, Sokolova J, Kraus E, Kraus JP, Kozich V. Impaired heme binding and aggregation of mutant cystathionine beta-synthase subunits in homocystinuria. Am J Hum Genet. 2001 Jun;68(6):1506-13. Epub 2001 May 15. PMID:11359213 doi:10.1086/320597
↑ Castro R, Heil SG, Rivera I, Jakobs C, de Almeida IT, Blom HJ. Molecular genetic analysis of the cystathionine beta-synthase gene in Portuguese homocystinuria patients: three novel mutations. Clin Genet. 2001 Aug;60(2):161-3. PMID:11553052
↑ Maclean KN, Gaustadnes M, Oliveriusova J, Janosik M, Kraus E, Kozich V, Kery V, Skovby F, Rudiger N, Ingerslev J, Stabler SP, Allen RH, Kraus JP. High homocysteine and thrombosis without connective tissue disorders are associated with a novel class of cystathionine beta-synthase (CBS) mutations. Hum Mutat. 2002 Jun;19(6):641-55. PMID:12007221 doi:10.1002/humu.10089
↑ Gaustadnes M, Wilcken B, Oliveriusova J, McGill J, Fletcher J, Kraus JP, Wilcken DE. The molecular basis of cystathionine beta-synthase deficiency in Australian patients: genotype-phenotype correlations and response to treatment. Hum Mutat. 2002 Aug;20(2):117-26. PMID:12124992 doi:10.1002/humu.10104
↑ Urreizti R, Balcells S, Rodes M, Vilarinho L, Baldellou A, Couce ML, Munoz C, Campistol J, Pinto X, Vilaseca MA, Grinberg D. Spectrum of CBS mutations in 16 homocystinuric patients from the Iberian Peninsula: high prevalence of T191M and absence of I278T or G307S. Hum Mutat. 2003 Jul;22(1):103. PMID:12815602 doi:10.1002/humu.9153
↑ Kruger WD, Wang L, Jhee KH, Singh RH, Elsas LJ 2nd. Cystathionine beta-synthase deficiency in Georgia (USA): correlation of clinical and biochemical phenotype with genotype. Hum Mutat. 2003 Dec;22(6):434-41. PMID:14635102 doi:10.1002/humu.10290
↑ Orendae M, Pronicka E, Kubalska J, Janosik M, Sokolova J, Linnebank M, Koch HG, Kozich V. Identification and functional analysis of two novel mutations in the CBS gene in Polish patients with homocystinuria. Hum Mutat. 2004 Jun;23(6):631. PMID:15146473 doi:10.1002/humu.9249
↑ Linnebank M, Janosik M, Kozich V, Pronicka E, Kubalska J, Sokolova J, Linnebank A, Schmidt E, Leyendecker C, Klockgether T, Kraus JP, Koch HG. The cystathionine beta-synthase (CBS) mutation c.1224-2A>C in Central Europe: Vitamin B6 nonresponsiveness and a common ancestral haplotype. Hum Mutat. 2004 Oct;24(4):352-3. PMID:15365998 doi:10.1002/humu.9280
↑ Porto MP, Galdieri LC, Pereira VG, Vergani N, da Rocha JC, Micheletti C, Martins AM, Perez AB, Almeida VD. Molecular analysis of homocystinuria in Brazilian patients. Clin Chim Acta. 2005 Dec;362(1-2):71-8. Epub 2005 Jul 5. PMID:15993874 doi:10.1016/j.cccn.2005.05.030
↑ Lee SJ, Lee DH, Yoo HW, Koo SK, Park ES, Park JW, Lim HG, Jung SC. Identification and functional analysis of cystathionine beta-synthase gene mutations in patients with homocystinuria. J Hum Genet. 2005;50(12):648-54. Epub 2005 Oct 5. PMID:16205833 doi:10.1007/s10038-005-0312-2
↑ Urreizti R, Asteggiano C, Cozar M, Frank N, Vilaseca MA, Grinberg D, Balcells S. Functional assays testing pathogenicity of 14 cystathionine-beta synthase mutations. Hum Mutat. 2006 Feb;27(2):211. PMID:16429402 doi:10.1002/humu.9395
↑ Cozar M, Urreizti R, Vilarinho L, Grosso C, Dodelson de Kremer R, Asteggiano CG, Dalmau J, Garcia AM, Vilaseca MA, Grinberg D, Balcells S. Identification and functional analyses of CBS alleles in Spanish and Argentinian homocystinuric patients. Hum Mutat. 2011 Jul;32(7):835-42. doi: 10.1002/humu.21514. Epub 2011 Jun 7. PMID:21520339 doi:10.1002/humu.21514
↑ Kwok JS, Fung SL, Lui GC, Law EL, Chan MH, Leung CB, Tang NL. CBS gene mutations found in a Chinese pyridoxine-responsive homocystinuria patient. Pathology. 2011 Jan;43(1):81-3. doi: 10.1097/PAT.0b013e3283419dbb. PMID:21240075 doi:10.1097/PAT.0b013e3283419dbb
↑ McCorvie TJ, Kopec J, Hyung SJ, Fitzpatrick F, Feng X, Termine D, Strain-Damerell C, Vollmar M, Fleming J, Janz JM, Bulawa C, Yue WW. Inter-Domain Communication Of Human Cystathionine Beta Synthase: Structural Basis Of S-Adenosyl-L-Methionine Activation. J Biol Chem. 2014 Oct 21. pii: jbc.M114.610782. PMID:25336647 doi:http://dx.doi.org/10.1074/jbc.M114.610782

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==Crystal structure of human cystathionine beta-synthase (delta516-525) at 2.0 angstrom resolution==
-<StructureSection load='4coo' size='340' side='right' caption='[[4coo]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='4coo' size='340' side='right'caption='[[4coo]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4coo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4COO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4COO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4coo]] is a 2 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=4COO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4COO FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PE4:2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL'>PE4</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cystathionine_beta-synthase Cystathionine beta-synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.22 4.2.1.22] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PE4:2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL'>PE4</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></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=4coo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4coo OCA], [http://pdbe.org/4coo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4coo RCSB], [http://www.ebi.ac.uk/pdbsum/4coo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4coo ProSAT]</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=4coo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4coo OCA], [https://pdbe.org/4coo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4coo RCSB], [https://www.ebi.ac.uk/pdbsum/4coo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4coo ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/CBS_HUMAN CBS_HUMAN]] Defects in CBS are the cause of cystathionine beta-synthase deficiency (CBSD) [MIM:[http://omim.org/entry/236200 236200]]. CBSD is an enzymatic deficiency resulting in altered sulfur metabolism and homocystinuria. The clinical features of untreated homocystinuria due to CBS deficiency include myopia, ectopia lentis, mental retardation, skeletal anomalies resembling Marfan syndrome, and thromboembolic events. Light skin and hair can also be present. Biochemical features include increased urinary homocystine and methionine.<ref>PMID:1301198</ref> <ref>PMID:8353501</ref> <ref>PMID:7506602</ref> <ref>PMID:7981678</ref> <ref>PMID:7849717</ref> <ref>PMID:7967489</ref> <ref>PMID:7611293</ref> <ref>PMID:7762555</ref> <ref>PMID:7635485</ref> <ref>PMID:8528202</ref> <ref>PMID:7564249</ref> <ref>PMID:8755636</ref> <ref>PMID:8803779</ref> <ref>PMID:9156316</ref> <ref>PMID:9361025</ref> <ref>PMID:8990018</ref> <ref>PMID:9266356</ref> <ref>PMID:10462600</ref> <ref>PMID:10215408</ref> <ref>PMID:9889017</ref> <ref>PMID:10408774</ref> <ref>PMID:11013450</ref> <ref>PMID:11359213</ref> <ref>PMID:11553052</ref> <ref>PMID:12007221</ref> <ref>PMID:12124992</ref> <ref>PMID:12815602</ref> <ref>PMID:14635102</ref> <ref>PMID:15146473</ref> <ref>PMID:15365998</ref> <ref>PMID:15993874</ref> <ref>PMID:16205833</ref> <ref>PMID:16429402</ref> <ref>PMID:21520339</ref> <ref>PMID:21240075</ref>
+[https://www.uniprot.org/uniprot/CBS_HUMAN CBS_HUMAN] Defects in CBS are the cause of cystathionine beta-synthase deficiency (CBSD) [MIM:[https://omim.org/entry/236200 236200]. CBSD is an enzymatic deficiency resulting in altered sulfur metabolism and homocystinuria. The clinical features of untreated homocystinuria due to CBS deficiency include myopia, ectopia lentis, mental retardation, skeletal anomalies resembling Marfan syndrome, and thromboembolic events. Light skin and hair can also be present. Biochemical features include increased urinary homocystine and methionine.<ref>PMID:1301198</ref> <ref>PMID:8353501</ref> <ref>PMID:7506602</ref> <ref>PMID:7981678</ref> <ref>PMID:7849717</ref> <ref>PMID:7967489</ref> <ref>PMID:7611293</ref> <ref>PMID:7762555</ref> <ref>PMID:7635485</ref> <ref>PMID:8528202</ref> <ref>PMID:7564249</ref> <ref>PMID:8755636</ref> <ref>PMID:8803779</ref> <ref>PMID:9156316</ref> <ref>PMID:9361025</ref> <ref>PMID:8990018</ref> <ref>PMID:9266356</ref> <ref>PMID:10462600</ref> <ref>PMID:10215408</ref> <ref>PMID:9889017</ref> <ref>PMID:10408774</ref> <ref>PMID:11013450</ref> <ref>PMID:11359213</ref> <ref>PMID:11553052</ref> <ref>PMID:12007221</ref> <ref>PMID:12124992</ref> <ref>PMID:12815602</ref> <ref>PMID:14635102</ref> <ref>PMID:15146473</ref> <ref>PMID:15365998</ref> <ref>PMID:15993874</ref> <ref>PMID:16205833</ref> <ref>PMID:16429402</ref> <ref>PMID:21520339</ref> <ref>PMID:21240075</ref>
 == Function ==
-[[http://www.uniprot.org/uniprot/CBS_HUMAN CBS_HUMAN]] Only known pyridoxal phosphate-dependent enzyme that contains heme. Important regulator of hydrogen sulfide, especially in the brain, utilizing cysteine instead of serine to catalyze the formation of hydrogen sulfide. Hydrogen sulfide is a gastratransmitter with signaling and cytoprotective effects such as acting as a neuromodulator in the brain to protect neurons against hypoxic injury (By similarity).
+[https://www.uniprot.org/uniprot/CBS_HUMAN CBS_HUMAN] Only known pyridoxal phosphate-dependent enzyme that contains heme. Important regulator of hydrogen sulfide, especially in the brain, utilizing cysteine instead of serine to catalyze the formation of hydrogen sulfide. Hydrogen sulfide is a gastratransmitter with signaling and cytoprotective effects such as acting as a neuromodulator in the brain to protect neurons against hypoxic injury (By similarity).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 21: @@
 </div>
 <div class="pdbe-citations 4coo" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Cystathionine ÃÂ²-synthase 3D structures|Cystathionine ÃÂ²-synthase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Cystathionine beta-synthase]]
+[[Category: Homo sapiens]]
-[[Category: Human]]
+[[Category: Large Structures]]
-[[Category: Arrowsmith, C]]
+[[Category: Arrowsmith C]]
-[[Category: Bountra, C]]
+[[Category: Bountra C]]
-[[Category: Bradley, A]]
+[[Category: Bradley A]]
-[[Category: Burgess-Brown, N]]
+[[Category: Burgess-Brown N]]
-[[Category: Bushell, S]]
+[[Category: Bushell S]]
-[[Category: Carpenter, E S]]
+[[Category: Carpenter ES]]
-[[Category: Delft, F von]]
+[[Category: Edwards A]]
-[[Category: Edwards, A]]
+[[Category: Froese DS]]
-[[Category: Froese, D S]]
+[[Category: Kiyani W]]
-[[Category: Kiyani, W]]
+[[Category: Kopec J]]
-[[Category: Kopec, J]]
+[[Category: McCorvie TJ]]
-[[Category: McCorvie, T J]]
+[[Category: Strain-Damerell C]]
-[[Category: Strain-Damerell, C]]
+[[Category: Tallant C]]
-[[Category: Tallant, C]]
+[[Category: Vollamar M]]
-[[Category: Vollamar, M]]
+[[Category: Yue WW]]
-[[Category: Yue, W W]]
+[[Category: Von Delft F]]
-[[Category: Allosteric regulation]]
-[[Category: Lyase]]
-[[Category: Metabolic pathway]]
-[[Category: Methionine cycle]]
-[[Category: Serine metabolism]]

4coo

From Proteopedia

Current revision

Crystal structure of human cystathionine beta-synthase (delta516-525) at 2.0 angstrom resolution

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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