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| <StructureSection load='1lgn' size='340' side='right' caption='Structure of human pentameric SAP (green, grey, pink, yellow, magenta) complex with AMP and Ca+2 ions (green) (PDB code [[1lgn]])' scene='87/875651/Cv/1'> | | <StructureSection load='4ht9' size='340' side='right' caption='Structure of E. coli hexameric Hfq complex with poly(A) RNA and poly(U) RNA (PDB code [[4ht9]])' scene='87/875687/Cv/1'> |
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| == Function == | | == Function == |
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| '''Serum amyloid P-component''' (SAP) is a plasma protein and is the precursor of amyloid P-component which is constituent of deposits in amyloidosis and Alzheimer disease<ref>PMID:8202534</ref>. SAP binds in a calcium-dependent fashion to a variety of ligands. | | '''Protein Hfq''' (Hfq) ('''H'''ost '''F'''actor for '''Q'''β) or '''RNA-binding protein Hfq''' is stimulating base-pairing between sRNA and target mRNA by binding both RNAs via three RNA-binding surfaces. Hfq is found in enteric bacteria<ref>PMID:30487269</ref>. Hfq binds RNA via poly(A-R-N) triplets where A is adenosine, R is purine nucleotide and N is any nucleotide<ref>PMID:19889981</ref>. |
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| == Relevance == | | == Relevance == |
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| Mutations in SAP affect the aggregation of mutated lysozyme which cause amyloidosis. The inhibition of SAP binding to amyloid fibrils is a therapeutic target in some serious human diseases<ref>PMID:26176329</ref>. Small molecule ligands can displace SAP from amyloid fibrils and can provide therapeutic treatment of amyloidosis.
| | Since Hfq is required for gene regulation and infectivity of some Gram-negative bacteria its mutations can eliminate infectivity of Lyme disease caused by the bacteria ''Borellia burgdorferi,'' for example<ref>PMID:20815822</ref>. |
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| == Structural highlights == | | == Structural highlights == |
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| <scene name='87/875651/Cv/5'>The 3D structure of a complex of SAP with the small molecule ligand AMP</scene> shows the nucleotide phosphate group bridging two Ca+2 ions and forming hydrogen bonds to Asn, Gln and Try residues of SAP <ref>PMID:9217261</ref>. | | The biological assembly of Protein Hfq from ''E. coli'' is <scene name='87/875687/Cv/2'>homohexamer</scene> (PDB code [[4ht9]]). The 3D structure of the complex between Hfq and <scene name='87/875687/Cv/5'>poly(A) RNA and poly(U) RNA</scene> shows the poly(A) binding at the distal face of Hfq and poly(U) binding at its proximal face. For the poly(A) A-R-N binding site the A site shows <scene name='87/875687/Cv/4'>hydrogen bonding to Gln and Lys</scene>. The <scene name='87/875687/Cv/6'>R site shows stacking interactions as well as hydrogen bonding</scene>. The N site does not show any interaction. <scene name='87/875687/Cv/7'>The poly(U) binding site of Hfq is a classical uridine binding pocket with both stacking and hydrogen bonding interactions</scene><ref>PMID:23605038</ref>. |
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| </StructureSection>
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| == 3D Structures of protein Hfq == | | == 3D Structures of protein Hfq == |
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| Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
| | [[Protein Hfq 3D structures]] |
| {{#tree:id=OrganizedByTopic|openlevels=0|
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| *Protein Hfq
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| **[[1hk9]], [[2y90]], [[2yht]], [[3qhs]], [[4rcb]], [[4rcc]], [[6bdg]] – EcHfq – ''Escherichia coli'' <br />
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| **[[4jli]], [[4jri]], [[4jrk]], [[4juv]] – EcHfq (mutant)<br />
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| **[[1u1s]], [[1u1t]], [[4j6y]], [[6xyj]] – PaHfq – ''Pseudomonas aeruginosa''<br />
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| **[[3inz]], [[3m4g]], [[4mml]], [[4mmk]], [[5i21]] – PaHfq (mutant)<br />
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| **[[2ylb]] – StHfq – ''Salmonella typhimurium''<br />
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| **[[6gwk]] – Hfq – ''Caulobacter crescentus''<br />
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| **[[4nl2]] – LmHfq – ''Listeria monocytogenes''<br />
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| **[[4noy]] – LmHfq (mutant)<br />
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| **[[5szd]] – AaHfq – ''Aquifex aeolicus''<br />
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| **[[3sb2]] – Hfq - ''Herbaspirillum seropedicae''<br />
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| **[[1kq1]] – SaHfq – ''Staphylococcus aureus''<br />
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| **[[2qtx]], [[4x9c]] – MjHfq – ''Methanococcus jannaschii''<br />
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| **[[3hfn]] – Hfq - ''Anabaena''<br />
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| *Protein Hfq complex with nucleotide
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| **[[3res]] – EcHfq + ADP<br />
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| **[[3qo3]] – EcHfq + ATP<br />
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| **[[4pno]] – EcHfq + UMP<br />
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| **[[4j6x]] – PaHfq + UTP<br />
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| **[[3qui]] – PaHfq + ADPNP<br />
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| **[[4j5y]] – PaHfq + ATP<br />
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| **[[4j6w]] – PaHfq + CTP<br />
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| **[[2ylc]] – StHfq + UMP<br />
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| **[[5dy9]] – MjHfq (mutant) + AMP<br />
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| **[[4x9d]] – MjHfq + UMP<br />
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| *Protein Hfq other complexes
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| **[[6qlb]] – EcHfq + calpain <br />
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| **[[3vu3]] – EcHfq + catalase <br />
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| **[[3gib]], [[4ht8]] – EcHfq + poly(A)<br />
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| **[[4ht9]], [[5new]] – EcHfq + poly(A) + poly(U)<br />
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| **[[3rer]] – EcHfq + poly(U) + ADP<br />
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| **[[4qvc]], [[4qvd]] – EcHfq + RNA<br />
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| **[[5uk7]] – EcHfq + DNA<br />
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| **[[3ahu]], [[3hsb]] – Hfq + RNA – ''Bacillus subtilis''<br />
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| **[[6o1k]], [[6o1l]], [[6o1m]] – PaHfq + Crc + RNA – Cryo EM<br />
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| **[[4v2s]] – StHfq + sRNA<br />
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| **[[4y91]] – Hfq + poly(U) – ''Thermotoga maritima''<br />
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| **[[4nl3]] – LmHfq + poly(U) <br />
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| **[[5sze]] – AaHfq + poly(U) <br />
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| **[[1kq2]] – SaHfq + RNA <br />
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| }}
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| == References == | | == References == |
| <references/> | | <references/> |
| | | </StructureSection> |
| [[Category:Topic Page]] | | [[Category:Topic Page]] |