User:Estelle Blochouse/ Sandbox 1497

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Copper is one of the most important metal involed in multiple enzyme catalysed reactions as a cofactor. In living organisms its function is related to the redox property of the copper. However it is toxic at all co,ce,tration, from the lower to the higher, and it need to be strictly controled in living organisms by molecular mechanisms.^[1]

Contents 1 Function 2 Disease 3 Relevance 4 Structural highlights

Function

Multicopper oxidases are enzymes involved in copper homeostasis. Copper as many metal ions is used in multiple biological processes such as detoxification of oxygen free radicals and pigmentation. However copper present in a cell bot bounded to a protein if harmfull and can cause cellular damage. It need to be regulated.

Multicopper oxidase might also be involved in the regulation of metal transport.

Multicopper oxidases are abble to oxiise their substrate. They accept an electron in the and transfer it to the trinuclear copper centre. The dioxygen bind to the trinuclear center and recieve four electron. It is transformed into two molecules of water.^[2] Three copper centres exist that can be differentiate spectroscopically: Type 1 or blue (), type 2 or normal (Cu1004) and type 3 or coupled binuclear (1002 and 1003).^[3][4]

Disease

If the amino acids 500 and 501 are mutated from CH to SR, the residual activity and loss of resistance to copper. E. Coli die.

Relevance

Structural highlights

Multicopper Oxidase CueO 4e9s is a protein containing one chain with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	Figure 1: Acetate ion.[5] ,
Related:	4e9p, 4e9q, 4e9r, 4e9t
Gene:	cueO, yacK, b0123, JW0119 (ECOLI)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

In the chain, 5 ligands are present: an acetate ion and 4 copper ions.
Figure 2: Copper 1001[6]	Cu1001: The copper ion is bound thanks to 3 metal protein interactions with H443, H505 and C500, structure stabilised by L502, M510 by hydrogen bonds
Figure 3: Copper 1002[7]	Cu1002: 2 atoms of Cu, bonds twice by metal interaction (2x3) with 3 histidine : H501, H103, H141 stabilised by hydrophobic contact with W139
Figure 4: Copper 1003[8]	Cu1003: 2 CU bond with 3histidine : H499, H143, H448 by 2 metal interactions. h448 is stabilised by Pi interactions with [CU]1004 and H101
Figure 5: Copper 1004[9]	Cu1004: one single atome of CU bonds once by metal interactions with 2 H ( and one ACT[1005]) : H101 and H446 stabilised by Pi interactions with H103 and H448. [CU]1004 has Pi interactions with H103 and H448. H113 and H446 Pi interactions
Figure 6: Acetate ion 1005[10]	ACT[1005]: is linked by hydrogen bonds to G104 and G449

Cu1002, Cu1003, Cu1004 and ACT[1005] are near in the space, the 3 CU form a triangle.

</td><td>221</td><td>222</td><td>223</td><td>224</td><td>225</td><td>226</td><td>227</td><td>228</td><td>229</td><td>230</td><td>231</td><td>232</td><td>233</td><td>234</td><td>235</td><td>236</td><td>237</td><td>238</td><td>239</td><td>240</td><td>241</td><td>242</td><td>243</td><td>244</td><td>245</td><td>246</td><td>247</td><td>248</td><td>249</td><td>250</td><td>251</td><td>252</td><td>253</td><td>254</td><td>255</td><td>256</td><td>257</td><td>258</td><td>259</td><td>260</td><td>261</td><td>262</td><td>263</td><td>264</td><td>265</td><td>266</td><td>267</td><td>268</td>

<tr><td>Y</td><td>P</td><td>Q</td><td>H</td><td>A</td><td>A</td><td>P</td><td>R</td><td>G</td><td>W</td><td>L</td><td>R</td><td>L</td><td>R</td><td>L</td><td>L</td><td>N</td><td>G</td><td>C</td><td>N</td><td>A</td><td>R</td><td>S</td><td>L</td><td>N</td><td>F</td><td>A</td><td>T</td><td>S</td><td>D</td><td>N</td><td>R</td><td>P</td><td>L</td><td>Y</td><td>V</td><td>I</td><td>A</td><td>S</td><td>D</td><td>G</td><td>G</td><td>L</td><td>L</td><td>P</td><td>E</td><td>P</td><td>V</td></tr> KVSELPVLMGERFEVLVEVNDNKPFDLVTLPVSQMGMAIAPFDKPHPVMRIQPIAISASGALPDTLSSLPALPSLEGLTV RKLQLSMDPMLDMMGMQMLMEKYGDQAMAGMDHSQMMGHMGHGNMNHMNHGGKFDFHHANKINGQAFDMNKPMFAAAKGQ YERWVISGVGDMMLHPFHIHGTQFRILSENGKPPAAHRAGWKDTVKVEGNVSEVLVKFNHDAPKEHAYMAHCHLLEHEDT GMMLGFTVG </td></tr> </table>

AERPTLPIPDLLTTDARNRIQLTIGAGQSTFGGKTATTWGYNGNLLGPAVKLQRGKAVTVDIYNQLTEETTLHWHGLEVP

GEVDGGPQGIIPPGGKRSVTLNVDQPAATCWFHPHQHGKTGRQVAMGLAGLVVIEDDEILKLMLPKQWGIDDVPVIVQDK KFSADGQIDYQLDVMTAAVGWFGDTLLTNGAIYPQHAAPRGWLRLRLLNGCNARSLNFATSDNRPLYVIASDGGLLPEPV KVSELPVLMGERFEVLVEVNDNKPFDLVTLPVSQMGMAIAPFDKPHPVMRIQPIAISASGALPDTLSSLPALPSLEGLTV RKLQLSMDPMLDMMGMQMLMEKYGDQAMAGMDHSQMMGHMGHGNMNHMNHGGKFDFHHANKINGQAFDMNKPMFAAAKGQ YERWVISGVGDMMLHPFHIHGTQFRILSENGKPPAAHRAGWKDTVKVEGNVSEVLVKFNHDAPKEHAYMAHCHLLEHEDT GMMLGFTVG

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The amino acid sequence is:
29	30	31	32	33	34	35	36	37	38	39	40	41	42	43	44	45	46	47	48	49	50	51	52	53	54	55	56	57	58
A	E	R	P	T	L	P	I	P	D	L	L	T	T	D	A	R	N	R	I	Q	L	T	I	G	A	G	Q	S	T
59	60	61	62	63	64	65	66	67	68	69	70	71	72	73	74	75	76	77	78	79	80	81	82	83	84	85	86	87	88
F	G	G	K	T	A	T	T	W	G	Y	N	G	N	L	L	G	P	A	V	K	L	Q	R	G	K	A	V	T	V
89	90	91	92	93	94	95	96	97	98	99	100	101	102	103	104	105	106	107	108	109	110	111	112	113	114	115	116	117	118
D	I	Y	N	Q	L	T	E	E	T	T	L	H	W	H	G	L	E	V	P	G	E	V	D	G	G	P	Q	G	I
119	120	121	122	123	124	125	126	127	128	129	130	131	132	133	134	135	136	137	138	139	140	141	142	143	144	145	146	147	148
I	P	P	G	G	K	R	S	V	T	L	N	V	D	Q	P	A	A	T	C	W	F	H	P	H	Q	H	G	K
149	150	151	152	153	154	155	156	157	158	159	160	161	162	163	164	165	166	167	168	169	170	171	172	173	174	175	176	177	178
T	G	R	Q	V	A	M	G	L	A	G	L	V	V	I	E	D	D	E	I	L	K	L	M	L	P	K	Q	W	G
179	180	181	182	183	184	185	186	187	188	189	190	191	192	193	194	195	196	197	198	199	200	201	202	203	204	205	206	207	208
I	D	D	V	P	V	I	V	Q	D	K	K	F	S	A	D	G	Q	I	D	Y	Q	L	D	V	M	T	A	A	V	G	W	F	G	D	T	L	L	T	N	G	A	I
209	210	211	212	213	214	215	216	217	218	219	220

References

1. ↑ EMBL-EBI, Family: Cu-oxidase (PF00394), Summary: Multicopper oxidase, http://pfam.xfam.org/family/Cu-oxidase
2. ↑ <ref>PMID:9556453</ref>
3. ↑ <ref>PMID:9556453</ref>
4. ↑ <ref>PMID:9556453</ref>
5. ↑ RCSB PDB
6. ↑ RCSB PDB
7. ↑ RCSB PDB
8. ↑ RCSB PDB
9. ↑ RCSB PDB
10. ↑ RCSB PDB

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