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Figure 1 | BMC Structural Biology

Figure 1

From: The crystal structure of the catalytic domain of a eukaryotic guanylate cyclase

Figure 1

Structural alignment of selected guanylate and adenylate cyclase catalytic domains. Secondary structure annotation and numbering correspond to the guanylate cyclase homolog CYG12 from C. reinhardtii. Sequences are grouped as follows: A, atypical soluble guanylate cyclases; B, membrane-bound guanylate cyclases; C, NO-sensing soluble guanylate cyclases; D, putative bacterial guanylate cyclases; E, mammalian and bacterial adenylate cyclases. Functional residues are indicated by symbols: metal binding (*); ribose binding (Δ); guanine/adenine binding (); triphosphate binding (#). Accession numbers are as follows: Chlamydomonas reinhardtii CYG12 (GenBank XP_001700847), Caenorhabditis elegans GCY35 (GenBank O02298), Rattus norvegicus sGCβ2 (GenBank BAB68564), Drosophila melanogaster GYC-88E (GenBank Q8INF0), Homo sapiens RetGC1 (GenBank Q02846), R. norvegicus GCA (GenBank P18910), C. elegans GCY7 (GenBank AAQ62451), Strongylocentrotus purpuratus mGC (GenBank P16065), R. norvegicus sGCβ1 (GenBank BAC55087), Oryzias latipes sGCβ1 (GenBank BAA76691), Manduca sexta sGCβ1 (GenBank AAC61264), D. melanogaster sGCβ1 (GenBank), R. norvegicus sGCα1 (GenBank AAB17953), O. latipes sGCα1 (GenBank BAA76690), M. sexta sGCα1 (GenBank AAC61263), D. melanogaster sGCα1 (GenBank AAF56917), Anabaena sp. PCC7120 all1118 (GenBank NP_485161), Nostoc punctiforme PCC73102 NpR1313 (GenBank YP_001864972), N. punctiforme PCC73102 NpR0352 (GenBank ACC79135), Trichodesmium erythraeum IMS101 Tery_4585 (GenBank ABG53561), T. erythraeum IMS101 Tery_3412 (GenBank ABG52512), Synechocystis sp. PCC6803 sll0646 (GenBank BAA16969), Canis familiaris ACV_C1 (GenBank 1CJU_A), R. norvegicus ACII_C2 (GenBank 1CJU_B), Mycobacterium tuberculosis Rv1264 (GenBank 1Y11_A), M. tuberculosis Rv1900c (GenBank 1YBU_C), Spirulina platensis CyaC (GenBank 1WC1_C). Initial alignments were carried out using the program ClustalX [67]. Sequences were adjusted manually with comparison to results from a structural homology search using the DALI server [45]. Figure 1 was prepared using the program ESPRIPT [68]. Regions containing residues of > 70% equivalence (red letters) are boxed with a thin blue line, and absolutely conserved residues are highlighted in red.

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