User:Estelle Blochouse/ Sandbox 1497

From Proteopedia

(Difference between revisions)

Revision as of 23:43, 10 January 2019

Multicopper Oxidase CueO (4e9s)

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]

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.

<tr<</tr>

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	T
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
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	I
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
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
209	210	211	212	213	214	215	216	217	218	219	220	221	222	223	224	225	226	227	228	229	230	231	232	233	234	235	236	237	238
W	F	G	D	T	L	L	T	N	G	A	I	Y	P	Q	H	A	A	P	R	G	W	L	R	L	R	L	L	N	G
239	240	241	242	243	244	245	246	247	248	249	250	251	252	253	254	255	256	257	258	259	260	261	262	263	264	265	266	267	268
C	N	A	R	S	L	N	F	A	T	S	D	N	R	P	L	Y	V	I	A	S	D	G	G	L	L	P	E	P	V
269	270	271	272	273	274	275	276	277	278	279	280	281	282	283	284	285	286	287	288	289	290	291	292	293	294	295	296	297	298
K	V	S	E	L	P	V	L	M	G	E	R	F	E	V	L	V	E	V	N	D	N	K	P	F	D	L	V	T	L
299	300	301	302	303	304	305	306	307	308	309	310	311	312	313	314	315	316	317	318	319	310	321	322	323	324	325	326	327	328
P	V	S	Q	M	G	M	A	I	A	P	F	D	K	P	H	P	V	M	R	I	Q	P	I	A	I	S	A	S	G
329	330	331	332	333	334	335	336	337	338	339	340	341	342	343	344	345	346	347	348	349	350	351	352	353	354	355	356	357	358
A	L	P	D	T	L	S	S	L	P	A	L	P	S	L	E	G	L	T	V	R	K	L	Q	L	S	M	D	P	M
359	360	361	362	363	364	365	366	367	368	369	370	371	372	373	374	375	376	377	378	379	380	381	382	383	384	385	386	387	388
L	D	M	M	G	M	Q	M	L	M	E	K	Y	G	D	Q	A	M	A	G	M	D	H	S	Q	M	M	G	H	M
389	390	391	392	393	394	395	396	397	398	399	400	401	402	403	404	405	406	407	408	409	410	411	412	413	414	415	416	417	418
G	H	G	N	M	N	H	M	N	H	G	G	K	F	D	F	H	H	A	N	K	I	N	G	Q	A	F	D	M	N
419	420	421	422	423	424	425	426	427	428	429	430	431	432	433	434	445	436	437	438	439	440	441	442	443	444	445	446	447	448
K	P	M	F	A	A	A	K	G	Q	Y	E	R	W	V	I	S	G	V	G	D	M	M	L	H	P	F	H	I	H
449	450	451	452	453	454	455	456	457	458	459	460	461	462	463	464	465	466	467	468	469	470	471	472	473	474	475	476	477	478
G	T	Q	F	R	I	L	S	E	N	G	K	P	P	A	A	H	R	A	G	W	K	D	T	V	K	V	E	G	N
479	480	481	482	483	484	485	486	487	488	489	490	491	492	493	494	495	496	497	498	499	500	501	502	503	504	505	506	507	508
V	S	E	V	L	V	K	F	N	H	D	A	P	K	E	H	A	Y	M	A	H	C	H	L	L	E	H	E	D	T
509	510	511	512	513	514	515	516
G	M	M	L	G	F	T	V	G

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

References

↑ EMBL-EBI, Family: Cu-oxidase (PF00394), Summary: Multicopper oxidase, http://pfam.xfam.org/family/Cu-oxidase
↑ <ref>PMID:9556453</ref>
↑ <ref>PMID:9556453</ref>
↑ <ref>PMID:9556453</ref>
↑ RCSB PDB
↑ RCSB PDB
↑ RCSB PDB
↑ RCSB PDB
↑ RCSB PDB
↑ RCSB PDB

Proteopedia Page Contributors and Editors (what is this?)

Estelle Blochouse

Retrieved from "http://52.214.119.220/wiki/index.php/User:Estelle_Blochouse/_Sandbox_1497"

@@ Line 66: / Line 66: @@
 <tr><td>389</td><td>390</td><td>391</td><td>392</td><td>393</td><td>394</td><td>395</td><td>396</td><td>397</td><td>398</td><td>399</td><td>400</td><td>401</td><td>402</td><td>403</td><td>404</td><td>405</td><td>406</td><td>407</td><td>408</td><td>409</td><td>410</td><td>411</td><td>412</td><td>413</td><td>414</td><td>415</td><td>416</td><td>417</td><td>418</td></tr>
 <tr><td>G</td><td>H</td><td>G</td><td>N</td><td>M</td><td>N</td><td>H</td><td>M</td><td>N</td><td>H</td><td>G</td><td>G</td><td>K</td><td>F</td><td>D</td><td>F</td><td>H</td><td>H</td><td>A</td><td>N</td><td>K</td><td>I</td><td>N</td><td>G</td><td>Q</td><td>A</td><td>F</td><td>D</td><td>M</td><td>N</td></tr>
-<tr><td>419</td><td>420</td><td>421</td><td>422</td><td>423</td><td>424</td><td>425</td><td>426</td><td>427</td><td>428</td><td>429</td><td>4230</td><td>431</td><td>432</td><td>433</td><td>434</td><td>445</td><td>436</td><td>437</td><td>438</td><td>439</td><td>440</td><td>441</td><td>442</td><td>443</td><td>444</td><td>445</td><td>446</td><td>447</td><td>448</td></tr>
+<tr><td>419</td><td>420</td><td>421</td><td>422</td><td>423</td><td>424</td><td>425</td><td>426</td><td>427</td><td>428</td><td>429</td><td>430</td><td>431</td><td>432</td><td>433</td><td>434</td><td>445</td><td>436</td><td>437</td><td>438</td><td>439</td><td>440</td><td>441</td><td>442</td><td class="blue">443</td><td>444</td><td>445</td><td>446</td><td>447</td><td>448</td></tr>
 <tr><td>K</td><td>P</td><td>M</td><td>F</td><td>A</td><td>A</td><td>A</td><td>K</td><td>G</td><td>Q</td><td>Y</td><td>E</td><td>R</td><td>W</td><td>V</td><td>I</td><td>S</td><td>G</td><td>V</td><td>G</td><td>D</td><td>M</td><td>M</td><td>L</td><td>H</td><td>P</td><td>F</td><td>H</td><td>I</td><td>H</td>
 <tr><td>449</td><td>450</td><td>451</td><td>452</td><td>453</td><td>454</td><td>455</td><td>456</td><td>457</td><td>458</td><td>459</td><td>460</td><td>461</td><td>462</td><td>463</td><td>464</td><td>465</td><td>466</td><td>467</td><td>468</td><td>469</td><td>470</td><td>471</td><td>472</td><td>473</td><td>474</td><td>475</td><td>476</td><td>477</td><td>478</td></tr>

User:Estelle Blochouse/ Sandbox 1497

From Proteopedia

Revision as of 23:43, 10 January 2019

Multicopper Oxidase CueO (4e9s)

Contents

Function

Disease

Relevance

Structural highlights

References

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox