Modomics - A Database of RNA Modifications

ID Card:

Full name: Iron-binding protein iscA
Synonym: YfhF
GI: 16130453
Orf: b2528
COG: COG0316
UniProt: P0AAC8
Structures: | 1S98 | 1R94 | 1R95 |
Alpha Fold Predicted Structure: AF-P0AAC8-F1


PDB Structures:


1S98

Structure Description:

Title: Crystal Structure of IscA (MERCURY DERIVATIVE)
Classification: METAL TRANSPORT
Technique: X-Ray Diffraction
Resolution: 2.30
R value free: 0.263
R value observed: 0.231
R value work: 0.229

Abstract of the PDB Structure's related Publication:

IscA belongs to an ancient family of proteins responsible for iron-sulfur cluster assembly in essential metabolic pathways preserved throughout evolution. We report here the 2.3 A resolution crystal structure of Escherichia coli IscA, a novel fold in which mixed beta-sheets form a compact alpha-beta sandwich domain. In contrast to the highly mobile secondary structural elements within the bacterial Fe-S scaffold protein IscU, a protein which is thought to have a similar function, the great majority of the amino acids that are conserved in IscA homologues are located in elements that constitute a well-ordered fold. However, the 10-residue C-terminal tail segment that contains two invariant cysteines critical for the Fe-S-binding function of a cyanobacterial (Synechocystis PCC) IscA homologue is not ordered in our structure. In addition, the crystal packing reveals a helical assembly that is constructed from two possible tetrameric oligomers of IscA.

Download RCSB-PDB Structures:

Pdb Files   1R94.pdb   1R95.pdb   1S98.pdb  
Pdbx/mmCIF Files   1R94.cif   1R95.cif   1S98.cif  


Protein sequence:

MSITLSDSAAARVNTFLANRGKGFGLRLGVRTSGCSGMAYVLEFVDEPTPEDIVFEDKGVKVVVDGKSLQFLDGTQLDFVKEGLNEGFKFTNPNVKDECGCGESFHV

Comments:

IscA is a scaffold protein for the [Fe-S] clusters. It binds ferredoxin, iron and [2Fe-2S] clusters, and participates in the biosynthesis of iron-sulfur proteins, including (dimethylallyl)adenosine tRNA methylthiotransferase MiaB. IscA homolog in human is IscA1, however its function is not clear.





Alpha Fold Predicted Structure:






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Protein sequence:

M S I T L S D S A A A R V N T F L A N R G K G F G L R L G V R T S G C S G M A Y V L E F V D E P T P E D I V F E D K G V K V V V D G K S L Q F L D G T Q L D F V K E G L N E G F K F T N P N V K D E C G C G E S F H V
102030405060708090100MSITLSDSAAARVNTFLANRGKGFGLRLGVRTSGCSGMAYVLEFVDEPTPEDIVFEDKGVKVVVDGKSLQFLDGTQLDFVKEGLNEGFKFTNPNVKDECGCGESFHVSequenceHTSN

Enter the variants

Position

Original

Variant

Secondary Structure Alphabet

  • G: 3-turn helix (310helix)
  • H: α-helix
  • I: 𝝅-helix (5 - turn helix)
  • T: Hydrogen Bonded Turn
  • B: β-sheet
  • S: Bend
  • C: Coil (residues not present in any of the above conformations)
  • N: Not assigned

Download PDB Structures & DSSP Secondary Structures:

Alpha Fold Pdb Files   AF-P0AAC8-F1.pdb  
Alpha Fold Pdbx/mmCIF Files   AF-P0AAC8-F1.cif  
DSSP Secondary Structures   P0AAC8.dssp  





Publications:

Links:

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